Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Arc mutant I137A + H2O
?
-
monomeric mutant, degradation
-
-
?
Arc repressor + H2O
?
-
interaction of Arc substrates with HslU variants bearing mutations in the GYVG pore loop or the I domain, overview. N-terminal residues of Arc initially interact with the GYVG loop in the axial pore of HslU, while other portions of Arc contact disordered I-domain loops, residues 175-209, that project into the substrate-binding funnel above the pore
-
-
?
Arc-MYL-st11 + H2O
?
-
recombinant Arc fusion protein
-
-
?
Arc-MYL-st11 plus + H2O
?
-
recombinant Arc fusion protein
-
-
?
Arc-st11-ssrADD + H2O
?
-
Arc variants with a C-terminal ssrA tag (Arc-ssrA), the st11 tag and a mutant ssrA tag in which the terminal AA sequence is replaced by DD
-
-
?
Arc1-53-st11-titin-ssrA + H2O
?
-
recombinant truncated Arc fusion protein
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
barnase-DHFR fusion proteins + H2O
?
benzyloxycarbonyl-EVNL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-EVNL + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
carbobenzoxy-Gly-Gly-Leu-7-amido-4-methyl coumarin + H2O
carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methyl coumarin
-
the HslV peptidase alone shows a very weak peptidase activity towards carbobenzoxy-Gly-Gly-Leu-7-amido-4-methyl coumarin, but its activity increases 1-2 orders of magnitude when it binds to HslU in the presence of ATP
-
-
?
carbobenzoxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
carboxymethylated lactalbumin + H2O
?
-
-
-
-
?
DnaA204-protein + H2O
?
-
the degradation of the DnaA204 protein contributes to the temperature sensitivity of the dna204 strain
-
-
?
fusion protein of SulA and maltose-binding protein + H2O
?
-
-
-
-
?
gt1 + H2O
?
-
substrate of HslU
-
-
?
lambda CI repressor ext1-lambdacIN-RSEYE + H2O
?
-
-
-
-
?
lambda cI repressor mutant ext1-lambdacIN-ISVTL + H2O
?
-
a variant in which the C-terminal sequence is changed from RSEYE to ISVTL, to give ext1-lambdacIN-ISVTL, that HslUV degrades faster than the parental protein, ext1-lambdacIN-RSEYE, by 2fold increase in Vmax
-
-
?
N-carbobenzoxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
N-carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
N-carbobenzyloxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
N-carbobenzyloxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
puromycylpolypeptide + H2O
?
-
HslV and HslU interact and participate in the degradation of misfolded puromycylpolypeptides
-
-
?
RpoH + H2O
?
-
RpoH is a heat shock sigma transcription factor
-
-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
SulA mutant F10A + H2O
?
-
-
-
-
?
SulA mutant I37V + H2O
?
-
-
-
-
?
SulA mutant P8L + H2O
?
-
-
-
-
?
SulA-maltose binding protein-fusion protein + H2O
?
unfolded lactalbumin + H2O
?
-
HslV alone can efficiently degrade certain unfolded proteins, such as unfolded lactalbumin and lysozyme prepared by complete reduction of disulfide bonds, but not their native forms. HslV alone cleaves a lactalbumin fragment sandwiched by two thioredoxin molecules, indicating that it can hydrolyze the internal peptide bonds of lactalbumin. Uncomplexed HslV is inactive under normal conditions, but can degrade unfolded proteins when the ATP level is low, as it is during carbon starvation
-
-
?
unfolded lysozyme + H2O
?
-
HslV alone can efficiently degrade certain unfolded proteins, such as unfolded lactalbumin and lysozyme prepared by complete reduction of disulfide bonds, but not their native forms. HslV alone cleaved a lactalbumin fragment sandwiched by two thioredoxin molecules, indicating that it can hydrolyze the internal peptide bonds of lactalbumin. Uncomplexed HslV is inactive under normal conditions, but can degrade unfolded proteins when the ATP level is low, as it is during carbon starvation
-
-
?
additional information
?
-
alpha-casein + H2O
?
-
-
-
?
alpha-casein + H2O
?
-
degradation
-
-
?
alpha-casein + H2O
?
-
interaction via HslV intact active site
-
-
?
alpha-casein + H2O
?
-
the structural features of the GYVG motif increase degrading activity
-
-
?
Arc + H2O
?
-
-
-
?
Arc + H2O
?
-
degradation
-
-
?
Arc + H2O
?
-
repressor protein, specific degradation, especially at heat shock temperatures, recognition of sequences near the N-terminus of Arc and strong binding requiring Mg2+ and ATP for degradation
-
-
?
Arc + H2O
?
-
N-terminal residues of Arc are important for HslUV degradation
-
-
?
Arc-st11-ssrA + H2O
?
-
Arc variants with a C-terminal ssrA tag (Arc-ssrA), the st11 and ssrA tags (Arc-st11-ssrA)
-
-
?
Arc-st11-ssrA + H2O
?
-
wild-type HslU binds this fluorescent substrate with an average affinity, whereas the Y91A mutant variant shows no detectable binding. Tyr91 side chain plays an important role in allowing HslU to bind Arc-st11-ssrA
-
-
?
barnase-DHFR fusion proteins + H2O
?
-
-
-
-
?
barnase-DHFR fusion proteins + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
HslV alone cleaves to a much lesser extent than in presence of HslU
-
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
-
the N-terminal Thr active sites of HslV are involved in the communication between HslV and HslU in addition to its role in the catalysis of peptide bond cleavage
-
-
?
carbobenzoxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
-
-
-
?
carbobenzoxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
The HslV peptidase alone shows a very weak peptidase activity towards carbobenzoxy-Gly-Gly-Leu-7-amido-4-methyl coumarin, but its activity increases 1-2 orders of magnitude when it binds to HslU in the presence of ATP
-
-
?
casein + H2O
?
-
-
-
-
?
Insulin B-chain + H2O
?
-
-
-
-
?
Insulin B-chain + H2O
?
-
HslVU degrades insulin B-chain even more rapidly in the presence of ATPgammaS than with ATP
-
-
?
RcsA + H2O
?
-
positive regulator of capsule transcription, RcsA
-
-
?
RcsA + H2O
?
-
specific substrate degradation, the enzyme is involved in regulation of RcsA, a capsule synthesis activator, the ClpYQ protease acts as a secondary protease in degrading the Lon protease substrate RscA
-
-
?
RcsA + H2O
?
-
specific substrate degradation, the enzyme is involved in regulation of RcsA, a capsule synthesis activator
-
-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
?
SulA + H2O
?
-
degradation
-
-
?
SulA + H2O
?
-
specific substrate degradation
-
-
?
SulA + H2O
?
-
specific substrate degradation, the substrate is a cell division inhibitor
-
-
?
SulA + H2O
?
-
recombinant substrate, produced as maltose-binding fusion protein and cleaved by factorXa
-
-
?
SulA + H2O
?
-
the double loops, i.e amino acids 137 to 150 and 175 to 209, in domain I of ClpY are necessary for initial recognition/tethering of natural substrates such as SulA, a cell division inhibitor protein
-
-
?
SulA + H2O
?
-
a cell division inhibitor protein. Degradation of MBP-SulA by ClpY and ClpY mutants Y408A and T87I in the presence of ClpQ
-
-
?
SulA + H2O
?
-
as MBP-SulA fusion protein
-
-
?
SulA + H2O
?
-
specific substrate degradation
-
-
?
SulA + H2O
?
-
specific substrate degradation, activities with SulA mutant protein substrates F10A, I37V, and P8L
-
-
?
SulA-maltose binding protein-fusion protein + H2O
?
-
recombinant substrate, formation of a ternary complex of HslV-HslU-substrate during reaction, molecular interaction study, interaction via HslU, not HslV
-
-
?
SulA-maltose binding protein-fusion protein + H2O
?
-
recombinant substrate, specific substrate degradation requires the flexibility provided by glycine residues and aromatic ring structures of the first 91 amino acids
-
-
?
TraJ + H2O
?
-
-
-
-
?
TraJ + H2O
?
-
TraJ appears to be a substrate for HslVU throughout the growth cycle, but is protected or modified by a factor encoded by the F transfer region in the absence of stress. Activation of the Cpx regulon destabilizes the F plasmid transfer activator, TraJ, via the HslVU protease
-
-
?
additional information
?
-
-
no hydrolysis of gamma-globulin, lysozyme and bovine serum albumin
-
-
?
additional information
?
-
-
HslV and HslU can function together as a novel ATP-dependent protease, the HslVU protease. Pure HslV is a weak peptidase degrading certain hydrophobic peptides. HslU dramatically stimulates peptide hydrolysis by HslV when ATP is present. With a 1:4 molar ratio of HslV to HslU, approximately a 200fold increase in peptide hydrolysis is observed. HslV stimulates the ATPase activity of HslU 2-4fold. CTP and dATP are slowly hydrolyzed by HslU and allow some peptide hydrolysis
-
-
?
additional information
?
-
-
ATP-binding, but not its hydrolysis, is essential for assembly and proteolytic activity of HslVU
-
-
?
additional information
?
-
-
less than 1% of the activity with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is observed with succinyl-AAF-7-amido-4-methylcoumarin and succinyl-LLVY-7-amido-4-methylcoumarin. No activity with benzoyl-RGFFL-4-methoxy-beta-naphthylamide, glutaryl-AAA-4-methoxy-beta-naphthylamide, benzyloxycarbonyl-LLE-4-methoxy-beta-naphthylamide, succinyl-FLF-beta-naphthylamide, succinyl-LY-7-amido-4-methylcoumarin, benzoyl-GP-7-amido-4-methylcoumarin, acetyl-YVAA-7-amido-4-methylcoumarin, tert-butyloxycarbonyl-LRR-7-amido-4-methylcoumarin, t-butyloxycarbonyl-FVR-7-amido-4-methylcoumarin, benzoyl-GGR-7-amido-4-methylcoumarin, benzoyl-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
hslV and hslU are coregulated. It is possible that ATPase HslU and protease HslV are involved in an ATP/GTP-dependent protein metabolism
-
-
?
additional information
?
-
-
the GYVG motif of HslU is important in unfolding of natively folded proteins as well as in translocation of unfolded proteins for degradation by HslV in its inner chamber
-
-
?
additional information
?
-
-
analysis of interaction of free and inhibited HslV with HslU showing moderate affinity, scheme of substrate-induced HslUV assemblage, overview
-
-
?
additional information
?
-
-
substrate binding, ATP-dependent protein degradation, and reaction mechanism, substrate engagement must occur after ATP-binding before HslUV unfolds the proteins, overview
-
-
?
additional information
?
-
-
degradation of proteins in an ATP-dependent and tag-specific manner. For degradation from the N-terminus, HslUV has the strongest unfolding ability of all the bacterial proteases (unfolding abilities of the 26S proteasome), whereas for degradation from the C-terminus, HslUV is one of the weaker unfoldases. HslUV unfolds proteins more effectively when degrading from the N- towards the C-terminus than in the opposite direction
-
-
?
additional information
?
-
-
HslVU is an ATP-dependent protease consisting of two heat shock proteins, the HslU ATPase and HslV peptidase. In the reconstituted enzyme, HslU stimulates the proteolytic activity of HslV by one to two orders of magnitude, while HslV increases the rate of ATP hydrolysis by HslU several-fold. HslV alone can efficiently degrade certain unfolded proteins, such as unfolded lactalbumin and lysozyme prepared by complete reduction of disulfide bonds, but not their native forms. HslV alone cleaves a lactalbumin fragment sandwiched by two thioredoxin molecules, indicating that it can hydrolyze the internal peptide bonds of lactalbumin. Uncomplexed HslV is inactive under normal conditions, but can degrade unfolded proteins when the ATP level is low, as it is during carbon starvation
-
-
?
additional information
?
-
-
ClpQ and ClpY are two heat shock proteins
-
-
?
additional information
?
-
-
in vivo, ClpYQ targets SulA, RcsA, RpoH, and TraJ molecules, identification of the molecular determinants required for the binding of its natural protein substrates by yeast two-hybrid analysis. Domain I of ClpY contains the residues, amino acids 137-150 of loop 1 and 175-209 of loop 2, double loops in domain I of ClpY, that are responsible for recognition of its natural substrates, while domain C is necessary to engage ClpQ, overview
-
-
?
additional information
?
-
-
ClpYQ is a two-component ATP-dependent protease in which ClpQ is the peptidase subunit and ClpY is the ATPase and the substrate-binding subunit. The ATP-dependent proteolysis is mediated by substrate recognition in the ClpYQ complex
-
-
?
additional information
?
-
-
HslVU is a bacterial ATP-dependent protease consisting of hexameric HslU ATPase and dodecameric HslV protease. HslV uses the N-terminal threonine as the active site residue. HslV has 12 active sites among the 14beta-subunits that can potentially contribute to proteolytic activity, but only 6 active sites are sufficient to support full catalytic activity. Substrate-mediated stabilization of the HslV-HslU interaction
-
-
?
additional information
?
-
-
HslU hexamers recognize and unfold native protein substrates and then translocate the polypeptide into the degradation chamber of the HslV peptidase. The degradation appears to consist of discrete steps, which involve the interaction of different terminal sequence signals in the substrate with different receptor sites in the HslUV protease. Mutations in the unstructured N-terminal and C-terminal sequences of two model substrates alter HslUV recognition and degradation kinetics, including changes in Vmax. Blocking either terminus of the substrate interferes with HslUV degradation, with synergistic effects when both termini are obstructed
-
-
?
additional information
?
-
-
modeling of overall reaction by substrate binding and dissociation steps, and by a rate-limiting enzymatic step, which corresponds to substrate engagement, unfolding, or translocation
-
-
?
additional information
?
-
-
substrates are typically targeted to specific AAA+ proteases by peptide sequences. In the AAA+ HslUV protease, substrates are bound and unfolded by a ring hexamer of HslU, before translocation through an axial pore and into the HslV degradation chamber. The I domain plays an active role in coordinating substrate binding, ATP hydrolysis, and protein degradation by the HslUV proteolytic machine
-
-
?
additional information
?
-
-
the enzyme degrades only the SulA moiety of recombinant fusion proteins, the fused proteins, e.g. the green fluorescent protein, are not hydrolyzed
-
-
?
additional information
?
-
-
degradation of proteins in an ATP-dependent and tag-specific manner. For degradation from the N-terminus, HslUV has the strongest unfolding ability of all the bacterial proteases (unfolding abilities of the 26S proteasome), whereas for degradation from the C-terminus, HslUV is one of the weaker unfoldases. HslUV unfolds proteins more effectively when degrading from the N- towards the C-terminus than in the opposite direction
-
-
?
additional information
?
-
-
the HslUV complex is an assembly of heat shock locus gene products U and V. The formation of the complete complex is essential for the proteasome to carry out its biochemical and physiological role in the parasite, namely to degrade specific target proteins in an ATP-dependent chaperone assisted manner
-
-
?
additional information
?
-
-
ClpYQ plays a minor role in stress survival and is required for growth at high temperature of 45°C
-
-
?
SulA + H2O
additional information
-
-
-
-
-
?
SulA + H2O
additional information
-
-
-
-
-
?
SulA + H2O
additional information
-
-
-
-
-
?
SulA + H2O
additional information
-
-
-
-
?
SulA + H2O
additional information
-
-
-
the enzyme produces 58 peptides with various sizes, 3-31 residues
?
SulA + H2O
additional information
-
-
the central and the C-terminal regions are preferentially cleaved. Major cleavage sites: Ala80-Ser81, Ala150-Ser151, Leu54-Gln55, Ile163-His164, Leu67-Thr68, Leu49-Leu50, Leu65-Trp66. No cleavage in absence of ATP
the enzyme produces 58 peptides with various sizes, 3-31 residues
?
SulA + H2O
additional information
-
-
cell division inhibitor SulA, the internal region of SulA is necessary for interactions with ClpY, the N-terminal amino acid residues of SulA are not necessary
-
-
?
SulA + H2O
additional information
-
-
hslVU in addition to Lon plays an important role in regulation of cell division through degradation of SulA
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
Escherichia coli HslUV protease is a member of a major family of ATP-dependent AAA+ degradation machines
malfunction
-
depletion of HslUV leads to an increase in the number of kinetoplasts which undergo abnormal segregation, causing the appearance of giant kinetoplasts as a result of the overreplication of minicircle DNA
physiological function
-
the enzyme is involved in a non-lysosomal degradation pathway important for Trypanosoma cruzi biology
physiological function
-
HslUV is involved in DNA replication and transcription
physiological function
-
HslUV is involved in DNA replication and transcription
physiological function
HslUV is involved in DNA replication and transcription
physiological function
-
HslV is essential for Leishmania donovani viability
physiological function
the protease complex subunits are involved in the control of cell cycle events
physiological function
Q4Q116; Q4QI03
the protease complex subunits are involved in the control of cell cycle events
physiological function
constrction of subunit HslU pseudohexamers containing mixtures of ATPase active and inactive subunits at defined positions in the hexameric ring. Genetic tethering impairs subunit HslV binding and degradation, even for pseudohexamers with six active subunits, but disulfide-linked pseudohexamers do not have these defects. Pseudohexamers containing different patterns of hydrolytically active and inactive subunits retain the ability to unfold protein substrates and/or collaborate with HslV in their degradation
physiological function
leptospiral HslUV is an ATP-dependent chaperone-peptidase complex containing ATPase associated with various cellular activity (AAA+) and N-terminal nucleophile (Ntn) hydrolase superfamily domains, respectively, which hydrolyzes casein and chymotrypsin-like substrates. Hydrolysis is blocked by threonine protease inhibitors. The infection of J774A.1 acrophages causes the increase of leptospiral denatured protein aggresomes, but more aggresomes accumulate in hslUV gene-deleted mutant. Compared to the wild-type strain, infection of cells in vitro with the mutant result in a higher number of dead leptospires, less leptospiral colonyforming units and lower growth ability, but also display a lower half lethal dose, attenuated histopathological injury and decreased leptospiral loading in lungs, liver, kidneys, peripheral blood and urine in hamsters
physiological function
protease HslV can be activated by peptides derived from the C-termini of both ATPase isoforms HslU1 and HslU2. Five out of the six C-terminal residues of HslU2 are essential for binding to and activating HslV. Dodecapeptides derived from HslU of other parasites and bacteria are able to activate HslV with similar or even higher efficiency
physiological function
-
the Hsp90 chaperone and the HslVU protease together regulate the level of TilS, involved in tRNA modification. Deletion of the genes coding for the HslVU protease suppresses the growth defect of an strain with hsp90 deleted, by increasing the cellular level of the essential TilS protein
physiological function
the shoot dry weight of Medicago sativa plants inoculated with Rhizobium meliloti HslU, HslV, HslUV or protease ClpXP1 deletion mutants is significantly reduced, and plants display slower free-living growth. All deletion mutants produce less exopolysaccharide and succinoglycan. Protease complexes HslUV and ClpXP are closely associated with ribosomal and proteome quality control proteins
physiological function
-
the enzyme is involved in a non-lysosomal degradation pathway important for Trypanosoma cruzi biology
-
physiological function
-
the protease complex subunits are involved in the control of cell cycle events
-
physiological function
-
the enzyme is involved in a non-lysosomal degradation pathway important for Trypanosoma cruzi biology
-
physiological function
-
the enzyme is involved in a non-lysosomal degradation pathway important for Trypanosoma cruzi biology
-
physiological function
-
the enzyme is involved in a non-lysosomal degradation pathway important for Trypanosoma cruzi biology
-
physiological function
-
the protease complex subunits are involved in the control of cell cycle events
-
physiological function
-
HslV is essential for Leishmania donovani viability
-
additional information
-
ClpYQ or HslUV is a two-component ATP-dependent protease composed of ClpY or HslU, an ATPase with unfolding activity, and ClpQ or HslV, a peptidase. In the ClpYQ proteolytic complex, the hexameric rings of ClpY (HslU) are responsible for protein recognition, unfolding, and translocation into the proteolytic inner chamber of the dodecameric ClpQ (HslV). The highly conserved sequence GYVG, residues 90 to 93, pore I site, along with the GESSG pore II site, residues 265 to 269, contribute to the central pore of ClpY in domain N. These two central loops of ClpY are in the center of its hexameric ring in which the energy of ATP hydrolysis allows substrate translocation and then degradation by ClpQ. The pore I site of ClpY has an effect on the adjoining structural region in protein substrates, and the pore I site is essential for the translocation of substrates. The pore II site also interfaces with nearby regions in the substrates but is not necessary for their translocation. An ATP-binding site in domain N, separate from its role in polypeptide, ClpY, oligomerization, is required for complex formation with ClpQ. Tyr408 in ClpY, like residue 385 in ClpX, is necessary for self-oligomerization, and this activity is likely important for in vivo protein-subunit stability
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A188S
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview
DELTA111-239
2 Gly linker, amidolytic ativity is 60-80% of the activity of the wild-type enzyme, caseinolytic activity is 60-80% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is 60-80% of the activity of the wild-type enzyme
DELTA137-150
2 Gly linker, amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are unchanged
DELTA175-209
2 Gly linker, amidolytic ativity, caseinolytic activity, and ATPase activity are unchanged, activity with the SalU-MBP fusion protein is less than 20% of the activity of the wild-type enzyme
DELTA423-443
5 Gly insertion, no amidolytic activity, no activity with casein and SulA-MBP fusion protein, no ATPase activity
DELTA88-92
3 Gly linker, amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are less than 20% of the activity of the wild-type enzyme
DELTA89-92
1 Gly linker, amidolytic ativity is 40-60% of the activity of the wild-type enzyme, caseinolytic activity is 40-60% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is 40-60% of the activity of the wild-type enzyme
E193L/E194L
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview
E266Q
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are unchanged
E266Q/E385
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are unchanged
E286Q
amidolytic ativity is 40-60% of the activity of the wild-type enzyme, caseinolytic activity is 40-60% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is 40-60% of the activity of the wild-type enzyme, ATPase activity is unchanged
E321Q
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity is less than 20% of the activity of the wild-type enzyme
E325E
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are less than 20% of the activity of the wild-type enzyme. Crystal structure of the mutant complex is nearly identical to then active complex
E436K/D437K
amidolytic ativity is 60-80% of the activity of the wild-type enzyme, caseinolytic activity is unchanged, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is unchanged
E88Q
amidolytic ativity is 20-40% of the activity of the wild-type enzyme, caseinolytic activity is less than 20% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is unchanged
E88Q/E266Q
amidolytic ativity is 20-40% of the activity of the wild-type enzyme, caseinolytic activity is less than 20% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is unchanged
E95W
amidolytic activity, activity with casein and ATPase activity are unchanged, activity with SulA-MBP fusion protein is 20-40% of the activity of the wild-type enzyme
G90P
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview, the mutant shows 41% reduced ATP hydrolysis activity compared to wild-type HslU
G93P
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
I186N
-
clpY mutant, the mutant does not interact with SulA compared to the wild-type ClpY
I312W
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are higher than the wild-type activities
Ins(435,436)
5 Gly insertion, no amidolytic activity, no activity with casein and SulA-MBP fusion protein, no ATPase activity
K80T
amidolytic ativity is 20-40% of the activity of the wild-type enzyme, caseinolytic activity is 40-60% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is unchanged, ATPase activity is unchanged
L88A
the mutation leads to a tighter binding between HslV and HslU and a dramatic stimulation of both the proteolytic and ATPase activities. Furthermore, the HslV mutant shows a more than 7fold increase of basal hydrolytic activities toward small peptides and unstructured proteins
L88F
the muattion increases the peptidolytic activity of HslV in both the absence and presence of HslU and stimulates the ATPase activity of HslU more than wild type HslV
L88G
the HslV mutant shows a marked increase of basal hydrolytic activities toward small peptides and unstructured proteins
L88S
the HslV mutant shows a marked increase of basal hydrolytic activities toward small peptides and unstructured proteins
L88W
the muattion increases the peptidolytic activity of HslV in both the absence and presence of HslU and stimulates the ATPase activity of HslU more than wild type HslV
M187I
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview
N141L/N142L
-
the ClpY loop 1 mutant is defective in complete degradation of SulA
N205K
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview
Q148L/Q149L/Q150L
-
the ClpY loop 1 mutant shows altered substrate recognition and binding, but shows normal activity similar to that of the wild-type ClpY
Q198L/Q200L
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview
Q311_I312insGGGGG
5 Gly insertion, amidolytic ativity, caseinolytic activity and activity with SulA-MBP fusion protein are less than 20% of the activity of the wild-type enzyme, ATPase activity is 20-40% of the activity of the wild-type enzyme
R393A
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity is less than 20% of the activity of the wild-type enzyme
R86A
the mutant shows little peptidolytic activity compared to the wild type
R86G
-
ATP inhibits the degradation of unfolded proteins by HslV. This inhibitory effect of ATP is markedly diminished by substitution of the Arg86 residue located in the apical pore of HslV with Gly
R89A
the mutant shows little peptidolytic activity compared to the wild type
S103A
50% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU
S124A
3% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU
S143A
95% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU
S172A
1% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU
S5A
124% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU
T387_E388insGGGGG
5 Gly insertion, amidolytic ativity is unchanged, caseinolytic activity is 60-80% of the activity of the wild-type enzyme, ATPase activity is unchanged
V92A
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
V92G
amidolytic activity, activity with casein and ATPase activity are unchanged, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme
V92I
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
V92S
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
Y91G
amidolytic ativity is 40-60% of the activity of the wild-type enzyme, caseinolytic activity is 40-60% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is unchanged
Y91S
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
DELTA83-92
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
DELTA86-91
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is unchanged
K28A
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
R35A
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
R86D
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
R89A/K90A
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
R89D
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is 40-60% of the activity of the wild-type enzyme
R89D/K90E
-
hydrolysis of casein and SulA-MBP is less than 20% of the activity of the wild-type enzyme, hydrolysis of benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is higher than that of the wild-type enzyme
V112A
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
G93A
amidolytic ativity is 20-40% of the activity of the wild-type enzyme, caseinolytic activity is 20-40% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is 40-60% of the activity of the wild-type enzyme
G93A
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
L199Q
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview. SulA accumulates in the bacterial cells that express ClpY
L199Q
substitution in I-domain of subunit HslU. Mutation does not alter the structure of the AAA+ ring or its interactions with HslV but increases I-domain susceptibility to limited endoproteolysis. The mutation increases the rate of ATP-hydrolysis substantially, results in slower degradation of some proteins but faster degradation of other substrates, and markedly changes the preference of HslUV for initiating degradation at the N-terminus or C-terminus of model substrates
Y91A
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
Y91A
-
site-directed mutagenesis of the HslU GYVG pore loop, the mutant shows no remaining activity, the mutant hydrolyzes ATP and stimulates HslV peptidase activity
Y91F
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
Y91F
-
site-directed mutagenesis of the HslU GYVG pore loop, the mutant shows reduced activity, the mutant hydrolyzes ATP and stimulates HslV peptidase activity
additional information
-
clpQ+Y+ promoter is fused to a lacZ reporter gene. The transcriptional or translational clpQ+::lacZ fusion gene is each crossed into lambda phage. The lambdaclpQ+::lacZ+, a transcriptional fusion gene, is used to form lysogens in the wild-type, rpoH or/and rpoS mutants. Upon shifting the temperature up from 30°C to 42°C, the wild-type transcriptional lambdaclpQ+::lacZ+ demonstrates an increased beta-galactosidase activity, overview. RpoH itself regulates clpQ+Y+ gene expression. The clpQ+Y+ message carries a conserved 71 bp at the 5'-untranslated region that is predicted to form the stem-loop structure by analysis of its RNA secondary structure
additional information
-
construction of mixed dodecamers having varied numbers of HslV and T1A subunits, and of a series of HslV dodecamers containing different numbers of active sites showing that HslV with only 6 active sites is sufficient to support full catalytic activity, a further reduction of the number of active sites leads to a proportional decrease in activity. Substrate-mediated stabilization of the HslV-HslU interaction remains unchanged until the number of the active sites is decreased to 6 but is gradually compromised upon further reduction. Deletion of Thr1 causes a dramatic increase in affinity between HslV and HslU
additional information
-
construction of truncation mutants lacking the substrate binding residues 137-209 of ClpY
additional information
-
construction of deletion mutants DELTA175-209linker, DELTA175-209GG, and DELTA108-243GG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Welch, R.A.; Burland, V.; Plunkett, G.III; Redford, P.; Roesch, P.; Rasko, D.; Buckles, E.L.; Liou, S.R.; Boutin, A.; Hackett, J.; Stroud, D.; Mayhew, G.F.; Rose, D.J.; Zhou, S.; Schwartz, D.C.; Perna, N.T.; Mobley, H.L.T.; Donnenberg, M.S.; Blattner, F.R.
Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli
Proc. Natl. Acad. Sci. USA
99
17020-17024
2002
Escherichia coli (P0A7B9)
brenda
Jin, Q.; Yuan, Z.; Xu, J.; Wang, Y.; et al.
Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157
Nucleic Acids Res.
30
4432-4441
2002
Shigella flexneri (P0A7C1), Shigella flexneri 301 (P0A7C1)
brenda
Plunkett, G.3rd; Burland, V.; Daniels, D.L.; Blattner, F.R.
Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes
Nucleic Acids Res.
21
3391-3398
1993
Escherichia coli (P0A7B8)
brenda
Perna, N.T.; Plunkett, G.; Burland, V.; Mau, B.; Glasner, J.D.; et al.
Genome sequence of enterohaemorrhagic Escherichia coli O157:H7
Nature
409
529-533
2001
Escherichia coli (P0A7C0)
brenda
Hayashi, T.; Makino, K.; Ohnishi, M.; Kurokawa, K.; Ishii, K.; et al.
Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12
DNA Res.
8
11-22
2001
Escherichia coli (P0A7C0)
brenda
Bochtler, M.; Ditzel, L.; Groll, M.; Huber, R.
Crystal structure of heat shock locus V (HslV) from Escherichia coli
Proc. Natl. Acad. Sci. USA
94
6070-6074
1997
Escherichia coli (P0A7B8), Escherichia coli
brenda
Bochtler, M.; Hartmann, C.; Song, H.K.; Bourenkov, G.P.; Bartunik, H.D.; Huber R.
The structures of HslU and the ATP-dependent protease HslU-HslV
Nature
403
800-805
2000
Escherichia coli (P0A7B8), Escherichia coli
brenda
Chuang, S.E.; Burland, V.; Plunkett, G.III; Daniels, D.L.; Blattner, F.R.
Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli
Gene
134
1-6
1993
Escherichia coli (P0A7B8)
brenda
Yoo, S.J.; Shim, Y.K.; Seong, I.S.; Seol, J.H.; Kang, M.S.; Chung, C.H.
Mutagenesis of two N-terminal Thr and five Ser residues in HslV, the proteolytic component of the ATP-dependent HslVU protease
FEBS Lett.
412
57-60
1997
Escherichia coli (P0A7B8), Escherichia coli
brenda
Yoo, S.J.; Seol, J.H.; Shin, D.H.; Rohrwild, M.; Kang, M.S.; Tanaka, K.; Goldberg, A.L.; Chung, C.H.
Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli
J. Biol. Chem.
271
14035-14040
1996
Escherichia coli
brenda
Yoo, S.J.; Seol, J.H.; Seong, I.S.; Kang, M.S.; Chung, C.H.
ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli
Biochem. Biophys. Res. Commun.
238
581-585
1997
Escherichia coli
brenda
Bochtler, M.; Song, H.K.; Hartmann, C.; Ramachandran, R.; Huber, R.
The quaternary arrangement of HslU and HslV in a cocrystal: a response to Wang, Yale
J. Struct. Biol.
135
281-293
2001
Escherichia coli
brenda
Bogyo, M.; McMaster, J.S.; Gaczynska, M.; Tortorella, D.; Goldberg, A.L.; Ploegh, H.
Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors
Proc. Natl. Acad. Sci. USA
94
6629-6634
1997
Escherichia coli
brenda
Huang, H.; Goldberg, A.L.
Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis
J. Biol. Chem.
272
21364-21372
1997
Escherichia coli
brenda
Lee, Y.Y.; Chang, C.F.; Kuo, C.L.; Chen, M.C.; Yu, C.H.; Lin, P.I.; Wu, W.F.
Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid system
J. Bacteriol.
185
2393-2401
2003
Escherichia coli
brenda
Seong, I.S.; Kang, M.S.; Choi, M.K.; Lee, J.W.; Koh, O.J.; Wang, J.; Eom, S.H.; Chung, C.H.
The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase
J. Biol. Chem.
277
25976-25982
2002
Escherichia coli
brenda
Nishii, W.; Takahashi, K.
Determination of the cleavage sites in SulA, a cell division inhibitor, by the ATP-dependent HslVU protease from Escherichia coli
FEBS Lett.
553
351-354
2003
Escherichia coli
brenda
Rohrwild, M.; Coux, O.; Huang, H.C.; Moerschell, R.P.; Yoo, S.J.; Seol, J.H.; Chung, C.H.; Goldberg, A.L.
HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome
Proc. Natl. Acad. Sci. USA
93
5808-5813
1996
Escherichia coli
brenda
Slominska, M.; Wahl, A.; Wegrzyn, G.; Skarstad, K.
Degradation of mutant initiator protein DnaA204 by proteases ClpP, ClpQ and Lon is prevented when DNA is SeqA-free
Biochem. J.
370
867-871
2003
Escherichia coli
brenda
Seong, I.S.; Oh, J.Y.; Yoo, S.J.; Seol, J.H.; Chung, C.H.
ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli
FEBS Lett.
456
211-214
1999
Escherichia coli
brenda
Song, H.K.; Hartmann, C.; Ramachandran, R.; Bochtler, M.; Behrendt, R.; Moroder, L.; Huber, R.
Mutational studies on HslU and its docking mode with HslV
Proc. Natl. Acad. Sci. USA
97
14103-14108
2000
Escherichia coli, Escherichia coli (Q8FBC0)
brenda
Wang, J.
A corrected quaternary arrangement of the peptidase HslV and atpase HslU in a cocrystal structure
J. Struct. Biol.
134
15-24
2001
Escherichia coli
brenda
Wang, J.; Song, J.J.; Franklin, M.C.; Kamtekar, S.; Im, Y.J.; Rho, S.H.; Seong, I.S.; Lee, C.S.; Chung, C.H.; Eom, S.H.
Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism
Structure
9
177-184
2001
Escherichia coli
brenda
Missiakas, D.; Schwager, F.; Betton, J.M.; Georgopoulos, C.; Raina, S.
Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli
EMBO J.
15
6899-6909
1996
Escherichia coli
brenda
Rohrwild, M.; Pfeifer, G.; Santarius, U.; Muller, S.A.; Huang, H.C.; Engel, A.; Baumeister, W.; Goldberg, A.L.
The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome
Nat. Struct. Biol.
4
133-139
1997
Escherichia coli
brenda
Kessel, M.; Wu, W.; Gottesman, S.; Kocsis, E.; Steven, A.C.; Maurizi, M.R.
Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY
FEBS Lett.
398
274-278
1996
Escherichia coli
brenda
Seol, J.H.; Yoo, S.J.; Shin, D.H.; Shim, Y.K.; Kang, M.S.; Goldberg, A.L.; Chung, C.H.
The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase
Eur. J. Biochem.
247
1143-1150
1997
Escherichia coli
brenda
Ramachandran, R.; Hartmann, C.; Song, H.K.; Huber, R.; Bochtler, M.
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY)
Proc. Natl. Acad. Sci. USA
99
7396-7401
2002
Haemophilus influenzae
brenda
Kwon, A.R.; Kessler, B.M.; Overkleeft, H.S.; McKay, D.B.
Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome
J. Mol. Biol.
330
185-195
2003
Haemophilus influenzae
brenda
Wei, J.; Goldberg, M.B.; Burland, V.; et al.
Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T
Infect. Immun.
71
2775-2786
2003
Shigella flexneri, Shigella flexneri 2457T / ATCC 700930
brenda
Wang, J.; Rho, S.H.; Park, H.H.; Eom, S.H.
Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects
Acta Crystallogr. Sect. D
61
932-941
2005
Bacillus subtilis, Escherichia coli
brenda
Frees, D.; Thomsen, L.E.; Ingmer, H.
Staphylococcus aureus ClpYQ plays a minor role in stress survival
Arch. Microbiol.
183
286-291
2005
Staphylococcus aureus
brenda
Park, E.; Rho, Y.M.; Koh, O.J.; Ahn, S.W.; Seong, I.S.; Song, J.J.; Bang, O.; Seol, J.H.; Wang, J.; Eom, S.H.; Chung, C.H.
Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase
J. Biol. Chem.
280
22892-22898
2005
Escherichia coli
brenda
Kwon, A.R.; Trame, C.B.; McKay, D.B.
Kinetics of protein substrate degradation by HslUV
J. Struct. Biol.
146
141-147
2004
Haemophilus influenzae
brenda
Kuo, M.S.; Chen, K.P.; Wu, W.F.
Regulation of RcsA by the ClpYQ (HslUV) protease in Escherichia coli
Microbiology
150
437-446
2004
Escherichia coli
brenda
Burton, R.E.; Baker, T.A.; Sauer, R.T.
Nucleotide-dependent substrate recognition by the AAA+ HslUV protease
Nat. Struct. Mol. Biol.
12
245-251
2005
Escherichia coli
brenda
Azim, M.K.; Goehring, W.; Song, H.K.; Ramachandran, R.; Bochtler, M.; Goettig, P.
Characterization of the HslU chaperone affinity for HslV protease. [Erratum to document cited in CA143:073777]
Protein Sci.
14
2484
2005
Escherichia coli
-
brenda
Lee, J.W.; Park, E.; Bang, O.; Eom, S.H.; Cheong, G.W.; Chung, C.H.; Seol, J.H.
Nucleotide triphosphates inhibit the degradation of unfolded proteins by HslV peptidase
Mol. Cell
23
252-257
2007
Escherichia coli
brenda
Lau-Wong, I.C.; Locke, T.; Ellison, M.J.; Raivio, T.L.; Frost, L.S.
HslVU protease
Mol. Microbiol.
67
516-527
2008
Escherichia coli
brenda
Azim, M.K.; Noor, S.
Characterization of protomer interfaces in HslV protease, the bacterial homologue of 20S proteasome
Protein J.
26
213-219
2007
Escherichia coli, Haemophilus influenzae, Thermotoga maritima
brenda
Rho, S.; Park, H.H.; Kang, G.B.; Im, Y.J.; Kang, M.S.; Lim, B.K.; Seong, I.S.; Seol, J.; Chung, C.H.; Wang, J.; Eom, S.H.
Crystal structure of Bacillus subtilis CodW, a noncanonical HslV-like peptidase with an impaired catalytic apparatus
Proteins Struct. Funct. Bioinform.
71
1020-1026
2008
Bacillus subtilis
brenda
Park, E.; Lee, J.W.; Eom, S.H.; Seol, J.H.; Chung, C.H.
Binding of MG132 or deletion of the Thr active sites in HslV subunits increases the affinity of HslV protease for HslU ATPase and makes this interaction nucleotide-independent
J. Biol. Chem.
283
33258-33266
2008
Escherichia coli
brenda
Koodathingal, P.; Jaffe, N.E.; Kraut, D.A.; Prakash, S.; Fishbain, S.; Herman, C.; Matouschek, A.
ATP-dependent proteases differ substantially in their ability to unfold globular proteins.
J. Biol. Chem.
284
18674-18684
2009
Escherichia coli, Haemophilus influenzae
brenda
Subramaniam, S.; Mohmmed, A.; Gupta, D.
Molecular modeling studies of the interaction between Plasmodium falciparum HslU and HslV subunits.
J. Biomol. Struct. Dyn.
26
473-479
2009
Plasmodium falciparum
brenda
Yakamavich, J.A.; Baker, T.A.; Sauer, R.T.
Asymmetric nucleotide transactions of the HslUV protease
J. Mol. Biol.
380
946-957
2008
Escherichia coli
brenda
Lee, J.W.; Park, E.; Bang, O.; Eom, S.H.; Cheong, G.W.; Chung, C.H.; Seol, J.H.
Nucleotide triphosphates inhibit the degradation of unfolded proteins by HslV peptidase
Mol. Cells
23
252-257
2007
Escherichia coli
brenda
Lien, H.Y.; Shy, R.S.; Peng, S.S.; Wu, Y.L.; Weng, Y.T.; Chen, H.H.; Su, P.C.; Ng, W.F.; Chen, Y.C.; Chang, P.Y.; Wu, W.F.
Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system
J. Bacteriol.
191
4218-4231
2009
Escherichia coli
brenda
Lee, J.W.; Park, E.; Jeong, M.S.; Jeon, Y.J.; Eom, S.H.; Seol, J.H.; Chung, C.H.
HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis
J. Biol. Chem.
284
33475-33484
2009
Escherichia coli
brenda
Lien, H.Y.; Yu, C.H.; Liou, C.M.; Wu, W.F.
Regulation of clpQY (hslVU) gene expression in Escherichia coli
Open Microbiol. J.
3
29-39
2009
Escherichia coli
brenda
Barboza, N.R.; Cardoso, J.; de Paula Lima, C.V.; Soares, M.J.; Gradia, D.F.; Hangai, N.S.; Bahia, M.T.; Lana, M.; Krieger, M.A.; Sa, R.G.
Expression profile and subcellular localization of HslV, the proteasome related protease from Trypanosoma cruzi
Exp. Parasitol.
130
171-177
2012
Trypanosoma cruzi, Trypanosoma cruzi Y, Trypanosoma cruzi Be-78, Trypanosoma cruzi Dcm28, Trypanosoma cruzi Be-62
brenda
Hsieh, F.C.; Chen, C.T.; Weng, Y.T.; Peng, S.S.; Chen, Y.C.; Huang, L.Y.; Hu, H.T.; Wu, Y.L.; Lin, N.C.; Wu, W.F.
Stepwise activity of ClpY (HslU) mutants in the processive degradation of Escherichia coli ClpYQ (HslUV) protease substrates
J. Bacteriol.
193
5465-5476
2011
Escherichia coli
brenda
Sundar, S.; McGinness, K.E.; Baker, T.A.; Sauer, R.T.
Multiple sequence signals direct recognition and degradation of protein substrates by the AAA+ protease HslUV
J. Mol. Biol.
403
420-429
2010
Escherichia coli
brenda
Sundar, S.; Baker, T.A.; Sauer, R.T.
The I domain of the AAA+ HslUV protease coordinates substrate binding, ATP hydrolysis, and protein degradation
Protein Sci.
21
188-198
2012
Escherichia coli
brenda
Mbang-Benet, D.E.; Sterkers, Y.; Morelle, C.; Kebe, N.M.; Crobu, L.; Portales, P.; Coux, O.; Hernandez, J.F.; Meghamla, S.; Pages, M.; Bastien, P.
The bacterial-like HslVU protease complex subunits are involved in the control of different cell cycle events in trypanosomatids
Acta Trop.
131
22-31
2014
Leishmania major (Q4Q116 and Q4QI03), Leishmania major, Leishmania major Friedlin (Q4Q116 and Q4QI03), Trypanosoma brucei (Q383Q5 and Q57VB1 and Q382V8), Trypanosoma brucei, Trypanosoma brucei 427 MiTat1.2 (Q383Q5 and Q57VB1 and Q382V8)
brenda
Rashid, Y.; Kamran Azim, M.; Saify, Z.S.; Khan, K.M.; Khan, R.
Small molecule activators of proteasome-related HslV peptidase
Bioorg. Med. Chem. Lett.
22
6089-6094
2012
Escherichia coli, Haemophilus influenzae (P43772)
brenda
Chrobak, M.; Foerster, S.; Meisel, S.; Pfefferkorn, R.; Foerster, F.; Clos, J.
Leishmania donovani HslV does not interact stably with HslU proteins
Int. J. Parasitol.
42
329-339
2012
Leishmania donovani, Leishmania donovani 1SR
brenda
Park, E.; Lee, J.W.; Yoo, H.M.; Ha, B.H.; An, J.Y.; Jeon, Y.J.; Seol, J.H.; Eom, S.H.; Chung, C.H.
Structural alteration in the pore motif of the bacterial 20S proteasome homolog HslV leads to uncontrolled protein degradation
J. Mol. Biol.
425
2940-2954
2013
Escherichia coli (P0A7B8), Escherichia coli
brenda
Ambro, L.; Pevala, V.; Bauer, J.; Kutejova, E.
The influence of ATP-dependent proteases on a variety of nucleoid-associated processes
J. Struct. Biol.
179
181-192
2012
Plasmodium falciparum, Trypanosoma brucei, Escherichia coli (P0A7B8)
brenda
Shi, L.; Kay, L.E.
Tracing an allosteric pathway regulating the activity of the HslV protease
Proc. Natl. Acad. Sci. USA
111
2140-2145
2014
Haemophilus influenzae
brenda
Dong, S.; Hu, W.; Ge, Y.; Ojcius, D.; Lin, X.; Yan, J.
A leptospiral AAA+ chaperone-Ntn peptidase complex, HslUV, contributes to the intracellular survival of Leptospira interrogans in hosts and the transmission of leptospirosis
Emerg. Microbes Infect.
6
e105
2017
Leptospira interrogans serovar Canicola (A0A0N7ELI3 and A0A0N9ELN0)
brenda
Kebe, N.M.; Samanta, K.; Singh, P.; Lai-Kee-Him, J.; Apicella, V.; Payrot, N.; Lauraire, N.; Legrand, B.; Lisowski, V.; Mbang-Benet, D.E.; Pages, M.; Bastien, P.; Kajava, A.V.; Bron, P.; Hernandez, J.F.; Coux, O.
The HslV protease from Leishmania major and its activation by C-terminal HslU peptides
Int. J. Mol. Sci.
20
1021
2019
Leishmania major (A4HWA6), Leishmania major
brenda
Ogden, A.; McAleer, J.; Kahn, M.
Characterization of the Sinorhizobium meliloti HslUV and ClpXP protease systems in free-living and symbiotic states
J. Bacteriol.
201
e00498
2019
Sinorhizobium meliloti (Q92TA7 and Q92TA9), Sinorhizobium meliloti
brenda
Baytshtok, V.; Chen, J.; Glynn, S.E.; Nager, A.R.; Grant, R.A.; Baker, T.A.; Sauer, R.T.
Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation
J. Biol. Chem.
292
5695-5704
2017
Escherichia coli (P0A6H5 and P0A7B8)
brenda
Honore, F.A.; Maillot, N.J.; Mejean, V.; Genest, O.
Interplay between the Hsp90 chaperone and the HslVU protease to regulate the level of an essential protein in Shewanella oneidensis
mBio
10
e00269
2019
Shewanella oneidensis
brenda
Baytshtok, V.; Fei, X.; Grant, R.A.; Baker, T.A.; Sauer, R.T.
A structurally dynamic region of the HslU intermediate domain controls protein degradation and ATP hydrolysis
Structure
24
1766-1777
2016
Escherichia coli (P0A6H5 and P0A7B8)
brenda