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the Pex1p/Pex6p-complex shows a dual localization in the cell as it is located in the cytosol as well as at the peroxisomal membrane
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the Pex1p/Pex6p complex exhibits a dual localization, with one fraction anchored to the peroxisomal membrane by its interaction to Pex15p and the second fraction located in the cytosol
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Pex15 is the membrane anchor required for Pex1/Pex6 recruitment to peroxisomes
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the peroxisomal proteins Pex1 and Pex6 form a heterohexameric type II AAA+ ATPase complex
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the Pex1p/Pex6p-complex shows a dual localization in the cell as it is located in the cytosol as well as at the peroxisomal membrane. Association of this complex with the peroxisomal membrane is mediated by binding to Pex15p. The predominant part of the tail anchored protein Pex15p faces the cytosol and mediates the peroxisomal membrane association of the AAA-complex via a direct interaction with the N-terminal domain of Pex6p, assembly of the Pex1p/Pex6p-complex and recruitment to the peroxisomal membrane
brenda
the Pex1p/Pex6p-complex shows a dual localization in the cell as it is located in the cytosol as well as at the peroxisomal membrane. Association of this complex with the peroxisomal membrane is mediated by binding to Pex15p. The predominant part of the tail-anchored protein Pex15p faces the cytosol and mediates the peroxisomal membrane association of the AAA-complex via a direct interaction with the N-terminal domain of Pex6p, assembly of the Pex1p/Pex6p-complex and recruitment to the peroxisomal membrane
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the Pex1p/Pex6p complex exhibits a dual localization, with one fraction anchored to the peroxisomal membrane by its interaction to Pex15p and the second fraction located in the cytosol
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Q9FNP1; Q8RY16
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structural organization and localization of peroxisomal AAA+ ATPases. The peroxisome specific isozyme is Lon2, which carries a PTS1-signal
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subcellular localization study using recombinant GFP-tagged enzyme expression
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AWP1 interacts with Pex6 on the peroxisome
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Pex1p is targeted to peroxisomes in a manner dependent on ATP hydrolysis. Transport of Pex1p and Pex6p is temperature-dependent
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Pex6p targeting to peroxisomes requires ATP but not its hydrolysis. Transport of Pex1p and Pex6p is temperature-dependent
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structural organization and localization of peroxisomal AAA+ ATPases. Dynamic Pex1p-Pex6p complex assembly at the peroxisomal membrane
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structural organization and localization of peroxisomal AAA+ ATPases. Dynamic Pex1p-Pex6p complex assembly at the peroxisomal membrane
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HpPln is localized in peroxisomes in Hansenula polymorpha, subcellular localization study
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structural organization and localization of peroxisomal AAA+ ATPases, peroxisomal matrix isozyme
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HpPln is localized in peroxisomes in Hansenula polymorpha, subcellular localization study
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structural organization and localization of peroxisomal AAA+ ATPases
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peroxisome-specific isoform of Lon protease, peroxisomal proteome analysis
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peroxisomal Pex1/Pex6 ATPase complex
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Pex1p is targeted to peroxisomes in a manner dependent on ATP hydrolysis, while Pex6p targeting requires ATP but not its hydrolysis
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structural organization and localization of peroxisomal AAA+ ATPases. Dynamic Pex1p-Pex6p complex assembly at the peroxisomal membrane
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additional information
four Lon isoforms localize to mitochondria, plastids and peroxisomes.The peroxisome specific enzyme is Lon2, which carries a PTS1-signal
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additional information
the tail-anchored protein Pex26p in humans functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex26p and mediates the attachment of the Pex1p-Pex6p complex to the membrane
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additional information
the tail-anchored protein Pex26p in humans functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex26p and mediates the attachment of the Pex1p-Pex6p complex to the membrane
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additional information
the tail-anchored protein Pex26p in humans functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex26p and mediates the attachment of the Pex1pPex6p complex to the membrane
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additional information
the tail-anchored protein Pex26p in humans functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex26p and mediates the attachment of the Pex1pPex6p complex to the membrane
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additional information
presence of two Lon isoforms with one of them located in the peroxisomal matrix
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additional information
immunohistochemic subcellular localization study
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additional information
the AAAdomains of Pex6p seem to influence the Pex6p/Pex15p-interaction and thereby regulate the recruitment of the cytosolic AAA-complex to the peroxisomal membrane, although in opposite fashion. In particular, ATP-binding to D1 of Pex6p stimulates association of the AAA-complex with Pex15p at the peroxisomal membrane while ATP-hydrolysis at D2 seems to trigger the release of the AAA-complex from Pex15p and thus from the membrane
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additional information
the AAAdomains of Pex6p seem to influence the Pex6p/Pex15p-interaction and thereby regulate the recruitment of the cytosolic AAA-complex to the peroxisomal membrane, although in opposite fashion. In particular, ATP-binding to D1 of Pex6p stimulates association of the AAA-complex with Pex15p at the peroxisomal membrane while ATP-hydrolysis at D2 seems to trigger the release of the AAA-complex from Pex15p and thus from the membrane
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additional information
the tail-anchored protein Pex15p in yeast functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex15p and mediates the attachment of the Pex1p-Pex6p complex to the membrane
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brenda
additional information
the tail-anchored protein Pex15p in yeast functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex15p and mediates the attachment of the Pex1p-Pex6p complex to the membrane
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brenda
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evolution
Arabidopsis contains four Lon protease-like proteins (AtLon1-AtLon4), predicted to be localized in different cellular organelles, including mitochondria, peroxisomes and plastids. AtLon2 is clustered in group II together with several Lon orthologues, which lack putative organelle N-terminal pre-sequences but contain the peroxisomal C-terminal localization signal, suggesting that plant orthologues within this group are localized to the peroxisomes
evolution
enzymes Pex1 and Pex6 are type-2 AAA+ ATPases
evolution
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases
evolution
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases
evolution
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases
evolution
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases
evolution
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases. Peroxismal Lon protease from Hansenula polymorpha shows 39% sequence identity with the putative peroxisomal Lon protease of Mus musculus
evolution
Pex1 and Pex6 are members of the AAA family of ATPases
evolution
Pex1p and Pex6p belong to the group of type-II AAA proteins characterized by the presence of two AAA-domains, termed D1 and D2, post-positioned to an N-terminal domain
evolution
the enzyme belongs to the a member of the Lon-family of proteases in the AAA+ ATPase superfamily, type I AAA+ ATPase
evolution
the enzyme belongs to the a member of the Lon-family of proteases in the AAA+ ATPase superfamily, type I AAA+ ATPase
evolution
the enzyme belongs to the a member of the Lon-family of proteases in the AAA+ ATPase superfamily, type I AAA+ ATPase
evolution
the enzyme belongs to the a member of the Lon-family of proteases in the AAA+ ATPase superfamily, type I AAA+ ATPase. Based on the domain composition and sequence characteristic of the domains, the Lon-proteases are subdivided into two classes, LonA and LonB. The LonA subfamily are soluble enzymes,which function in the bacterial cytosol and the mitochondrial matrix, whereas LonB predominates in Archaea
evolution
the enzyme belongs to the AAA+ ATPase family. AAA-proteins belong to the class of P-loop NTPases defined by conserved motifs for NTP-binding (Walker A motif) and hydrolysis (Walker B motif) which are assisted by Mg2+ as cofactor. Pex1p and Pex6p are evolutionary related to Cdc48p/p97
evolution
the enzyme belongs to the AAA+ ATPase superfamily
evolution
the enzyme belongs to the AAA+ ATPase superfamily
evolution
the enzyme belongs to the AAA+ ATPase superfamily
evolution
the enzyme belongs to the type II AAA+ ATPases, which by definition contain two conserved nucleotide-binding domains (D1 and D2) in tandem flanked by less conserved N- and C-terminal regions
evolution
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Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases. Peroxismal Lon protease from Hansenula polymorpha shows 39% sequence identity with the putative peroxisomal Lon protease of Mus musculus
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malfunction
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in fibroblasts from patients defective in Pex1, Pex6 and Pex26, (all of which are required for Pex5 export) Pex5 stability is decreased
malfunction
a deletion of peroxisomal Lon results in a specific growth defect on media containing oleic acid as a sole carbon source, conditions which require peroxisomal enzymes of the beta-oxidation pathway, the growth defect is accompanied by the formation of protein aggregates in the peroxisomal matrix
malfunction
a Lon protease deletion strain does not display a growth defect but a decreased viability of the cells
malfunction
a mutation of the conserved Walker A lysine in the D1 domain of Pex1, but not Pex6, dramatically affects the recovery of fully assembled recombinant hexamer
malfunction
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in cells of a PLN deletion strain, peroxisomes contain protein aggregates, a major component of which is catalase-peroxidase. Cells of the pln mutant strain contain enhanced levels of catalase-peroxidase protein but reduced catalase-peroxidase enzyme activities. And the absence of Pln results in the formation of protein aggregates in the peroxisomal matrix
malfunction
Lon2 absence leads to accumulation of enzymes in peroxisomes and results in an accelerated peroxisome degradation by pexophagy
malfunction
mutation of the Walker B motif in one D2 domain leads to ATP hydrolysis in the neighbouring domain
malfunction
mutations in the PEX1 gene, which encodes a protein required for peroxisome biogenesis, are themost common cause of the Zellweger spectrum diseases, the by far most abundant Pex1pG843D variation impairs the binding between Pex1p and Pex6p
malfunction
mutations in the proteins frequently cause peroxisomal diseases
malfunction
the absence of enzyme HpPln affects the viability of cells blocked in pexophagy, but does not affect cell growth. The number of peroxisomes is enhanced in enzyme deletion mutant cells
malfunction
the Arabidopsis apem10 mutant displays accelerated peroxisome degradation and a dramatically reduces number of peroxisomes. LON2 deficiency causes enhanced peroxisome degradation by autophagy, and peroxisomal proteins accumulates in the cytosol due to a decrease in the number of peroxisomes. The loss of function of LON2 leads to accelerated autophagy, accumulation of electron-dense inclusions in the peroxisome matrix and a delay in the elimination of glyoxysomal enzymes during post-germinative growth. apem10 phenotype, overview
malfunction
the PEX6-deletion strain has the most pronounced survival defects of all strains affected in peroxisome function
malfunction
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enzyme complex absence results in the selective degradation of the peroxisome. Loss of the enzyme complex does not prevent matrix protein import, but instead causes an upregulation of peroxisome degradation by macroautophagy, or pexophagy. The loss of enzyme complex function in cells results in the accumulation of ubiquitinated PEX5 on the peroxisomal membrane that signals pexophagy
malfunction
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mutations in Pex1 and Pex6 cause more than 80% of peroxisome biogenesis disorder cases, including Zellweger syndrome
malfunction
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mutations in Pex1 and Pex6 cause peroxisome biogenesis disorders
malfunction
Q9FNP1; Q8RY16
PEX6 mutants show growth defects, impaired matrix protein processing and decreased PEX5 levels
malfunction
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the receptor Pex5p is released from the membrane back to the cytosol in an ATP-dependent manner by the AAA-type ATPases Pex1p and Pex6p
malfunction
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in cells of a PLN deletion strain, peroxisomes contain protein aggregates, a major component of which is catalase-peroxidase. Cells of the pln mutant strain contain enhanced levels of catalase-peroxidase protein but reduced catalase-peroxidase enzyme activities. And the absence of Pln results in the formation of protein aggregates in the peroxisomal matrix
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malfunction
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the absence of enzyme HpPln affects the viability of cells blocked in pexophagy, but does not affect cell growth. The number of peroxisomes is enhanced in enzyme deletion mutant cells
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metabolism
the enzyme is involved in LON2- and autophagy-dependent degradation pathways during the functional transition of peroxisomes, two hypothetical mechanisms proposed for the functional transition of glyoxysomes to leaf peroxisomes, modeling
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis, proteins that play a role in peroxisome biogenesis are collectively called peroxins. Function of Pex1p and Pex6p in peroxisomal matrix protein import, overview
metabolism
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the enzyme is involved in the peroxisome quality control system
metabolism
turnover of peroxisomal enzymes may be regulated by a peroxisomal homologue of the mitochondrial Lon protease
metabolism
Q9FNP1; Q8RY16
a complex of the PEX1 and PEX6 ATPases and the PEX26 tail-anchored membrane protein removes ubiquitinated PEX5 from the peroxisomal membrane
metabolism
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Pex5p recognition by the peroxisomal AAA complex depends on the presence of the ubiquitin moiety and is mediated by enzyme Pex1p
metabolism
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the ATPases Pex1p and Pex6p form a heterohexameric complex, which is recruited to the peroxisomal import machinery by the membrane anchor protein Pex15p. The Pex1p/Pex6p complex recognizes the ubiquitinated import receptors, pulls them out of the membrane and releases them into the cytosol
metabolism
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the peroxisomal enzyme-complex is required to remove the ubiquitinated form of the shuttling peroxisomal matrix protein receptor, PEX5, from the peroxisomal membrane
metabolism
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the two AAA-ATPases Pex1p and Pex6p are required for biogenesis of peroxisomes. At the peroxisomal membrane, the enzyme complex is responsible for the release of the import receptor Pex5p at the end of the matrix protein import cycle
metabolism
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the enzyme is involved in the peroxisome quality control system
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physiological function
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results identify AWP1 as a novel cofactor of Pex6 involved in the regulation of Pex5 export during peroxisome biogenesis
physiological function
ATP hydrolysis at both Pex1p/Pex6p complex sites is needed for cell viability
physiological function
LON2 is involved in the peroxisomal functional transition and basal quality control of peroxisomes. Chaperone and protease functions of LON protease 2 modulate the peroxisomal transition and degradation with autophagy. Proteolytic consequence of LON2 for the degradation of peroxisomal proteins, unnecessary proteins are eliminated by LON2- and autophagy-dependent degradation pathways during the functional transition of peroxisomes. LON2 plays dual roles as an ATP-dependent protease and a chaperone. The chaperone domain of LON2 is essential for the suppression of autophagy, whereas its peptidase domain interferes with this chaperone function, indicating that intramolecular modulation between the proteolysis and chaperone functions of LON2 regulates degradation of peroxisomes by autophagy
physiological function
most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality
physiological function
most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality
physiological function
most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality
physiological function
most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality
physiological function
most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality, although the enzyme is not important for the viability
physiological function
Pex1 and Pex6 are required for the de novo biogenesis of peroxisomes. The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits. The recombinant Pex1-FLAG/His-Pex6 complex is an active ATPase
physiological function
Pex1p and Pex6p are crucial for peroxisome biogenesis, Pex6p functions together with Pex1p in peroxisome biogenesis. The ATP hydrolysis cycle of the AAA+-ATPases is supposed to regulate the assembly and disassembly of the Pex1p-Pex6p complex and its membrane association and release. Role of Pex1p in peroxisomal matrix protein import, overview
physiological function
Pex1p and Pex6p are crucial for peroxisome biogenesis, Pex6p functions together with Pex1p in peroxisome biogenesis. The ATP hydrolysis cycle of the AAA+-ATPases is supposed to regulate the assembly and disassembly of the Pex1p-Pex6p complex and its membrane association and release. Role of Pex1p/Pex6p in peroxisomal matrix protein import, overview
physiological function
Pex1p and Pex6p are crucial for peroxisome biogenesis, Pex6p functions together with Pex1p in peroxisome biogenesis. The ATP hydrolysis cycle of the AAA+-ATPases is supposed to regulate the assembly and disassembly of the Pex1p-Pex6p complex and its membrane association and release. Role of Pex6p in peroxisomal matrix protein import, overview
physiological function
Pex6p functions together with Pex1p in peroxisome biogenesis
physiological function
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Pln is an ATP-dependent protease that digests unfolded substrates e.g. oxidatively damaged catalase-peroxidase, and displays chaperone-like activity, circumventing accumulation of protein aggregates in peroxisomes that compromise organelle function. Peroxisomal proteostasis involves the Lon family protein that functions as protease and chaperone, Pln is crucial for peroxisome proteostasis
physiological function
the enzyme is essentially involved in peroxisome biogenesis, Pex1p provides the energy for import of peroxisomal matrix proteins. Peroxisomal matrix proteins are synthesized on free ribosomes in the cytosol and guided to the peroxisomal membrane by specific soluble receptors. At the membrane, the cargo-loaded receptors bind to a docking complex and the receptor-docking complex assembly is thought to form a dynamic pore which enables the transition of the cargo into the organellar lumen. The import cycle is completed by ubiquitination- and ATP-dependent dislocation of the receptor from the membrane to the cytosol, which is performed by the AAA-peroxins. Receptor ubiquitination and dislocation are the only energy-dependent steps in peroxisomal protein import. The export-driven import model suggests that the AAA-peroxins might function as motor proteins in peroxisomal import by coupling ATP-dependent removal of the peroxisomal import receptor and cargo translocation into the organelle
physiological function
the enzyme is essentially involved in peroxisome biogenesis, Pex6p provides the energy for import of peroxisomal matrix proteins. Peroxisomal matrix proteins are synthesized on free ribosomes in the cytosol and guided to the peroxisomal membrane by specific soluble receptors. At the membrane, the cargo-loaded receptors bind to a docking complex and the receptor-docking complex assembly is thought to form a dynamic pore which enables the transition of the cargo into the organellar lumen. The import cycle is completed by ubiquitination- and ATP-dependent dislocation of the receptor from the membrane to the cytosol, which is performed by the AAA-peroxins. Receptor ubiquitination and dislocation are the only energy-dependent steps in peroxisomal protein import. The export-driven import model suggests that the AAA-peroxins might function as motor proteins in peroxisomal import by coupling ATP-dependent removal of the peroxisomal import receptor and cargo translocation into the organelle. Pex6p might also have additional functions that appear not to be related to peroxisomes, yeast Pex6p acts as a suppressor for aging defects in mitochondria. Overexpression of Pex6p, but not of Pex1p, restores the import defect of mutant ATP2, the gene encoding the beta-subunit of mitochondrial F1,F0-ATPase, into mitochondria. Function for Pex6p in the prevention of necrotic cell death in yeast
physiological function
the enzyme is involved in peroxisome biogenesis abd associated with peroxisomal quality control. The Lon protease functions in the degradation of mutated or abnormal proteins as well as short-lived regulatory proteins, in particular those produced under stress conditions
physiological function
the enzyme is involved in peroxisome biogenesis and associated with peroxisomal quality control
physiological function
the enzyme is involved in peroxisome biogenesis and associated with peroxisomal quality control. Lon2 is required for the elimination of unnecessary proteins during the functional transition of glyoxysomes to peroxisomes
physiological function
the enzyme is involved in peroxisome biogenesis and associated with peroxisomal quality control. The peroxisomal Lon and autophagy function together in peroxisomal quality control
physiological function
the peroxisomal matrix protein import is facilitated by soluble receptor molecules which cycle between cytosol and the peroxisomal membrane. At the end of the receptor cycle, the import receptors are exported back to the cytosol in an ATP-dependent manner catalyzed by a complex of Pex1p and Pex6p
physiological function
the peroxisomal proteins Pex1 and Pex6 complex fuels essential protein transport across peroxisomal membranes. ATP hydrolysis results in a pumping motion of the complex, suggesting that Pex1/6 function involves substrate translocation through its central channel. ATPase activity of Pex6 D2 domains drive conformational changes, Pex1/6 movements during ATP binding and hydrolysis, overview
physiological function
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the enzyme complex Pex1/Pex6 plays a role in mechanical unfolding of peroxins or their extraction from the peroxisomal membrane during matrix-protein import
physiological function
Q9FNP1; Q8RY16
the enzyme complex plays a role in the import and export of peroxisomal proteins and in oil body utilization
physiological function
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the enzyme plays a role in many processes, including endoplasmic reticulum-associated protein degradation
physiological function
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the peroxisomal enzyme-complex is required for peroxisome quality control
physiological function
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the Pex1/Pex6 complex dislocates and recycles the transport receptor Pex5 from the peroxisomal membrane during peroxisomal protein import
physiological function
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Pln is an ATP-dependent protease that digests unfolded substrates e.g. oxidatively damaged catalase-peroxidase, and displays chaperone-like activity, circumventing accumulation of protein aggregates in peroxisomes that compromise organelle function. Peroxisomal proteostasis involves the Lon family protein that functions as protease and chaperone, Pln is crucial for peroxisome proteostasis
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physiological function
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most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality, although the enzyme is not important for the viability
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additional information
enzyme Pex1p/Pex6p complex structure modeling using a computational approach that combines Monte Carlo placement of structurally homologous domains into density maps with energy minimization and refinement protocols. Pex1 and Pex6 assemble into hexameric double rings and perform vital functions, structure-function relationship, molecular models. Comparison of the structures of the Pex1/Pex6 complex determined in presence of ATPgammaS and ADP
additional information
enzyme Pex1p/Pex6p complex structure modeling using a computational approach that combines Monte Carlo placement of structurally homologous domains into density maps with energy minimization and refinement protocols. Pex1 and Pex6 assemble into hexameric double rings and perform vital functions, structure-function relationship, molecular models. Comparison of the structures of the Pex1/Pex6 complex determined in presence of ATPgammaS and ADP
additional information
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molecular structure modeling
additional information
Pex1p and Pex6p interact and form a heteromeric complex. Disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion, indicating that formation of the Pex1p/Pex6p-complex requires the presence of ATP
additional information
Pex1p and Pex6p interact and form a heteromeric complex. Disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion, indicating that formation of the Pex1p/Pex6p-complex requires the presence of ATP
additional information
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Pex1p and Pex6p interact and form a heteromeric complex. Disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion, indicating that formation of the Pex1p/Pex6p-complex requires the presence of ATP
additional information
structural organization and localization of peroxisomal AAA+ ATPases
additional information
structural organization and localization of peroxisomal AAA+ ATPases
additional information
structural organization and localization of peroxisomal AAA+ ATPases
additional information
structural organization and localization of peroxisomal AAA+ ATPases
additional information
structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
structure-function analysis. AAA-peroxins defective in ATP-hydrolysis of D1 are at least partially functional. In contrast, ATP-hydrolysis of the conserved AAA-domains (D2) of both AAA-peroxins is essential for their function. The conserved D2-domains of Pex1p and Pex6p require hydrolysis of ATP for their function in peroxisome biogenesis, indicating that they may provide the driving force for conformational changes triggered by the AAA-peroxins
additional information
structure-function analysis. AAA-peroxins defective in ATP-hydrolysis of D1 are at least partially functional. In contrast, ATP-hydrolysis of the conserved AAA-domains (D2) of both AAA-peroxins is essential for their function. The conserved D2-domains of Pex1p and Pex6p require hydrolysis of ATP for their function in peroxisome biogenesis, indicating that they may provide the driving force for conformational changes triggered by the AAA-peroxins
additional information
structure-function analysis. The D1 of Pex6p does not contain a functional Walker B motif for ATP hydrolysis. AAA-peroxins defective in ATP-hydrolysis of D1 are at least partially functional. In contrast, ATP-hydrolysis of the conserved AAA-domains (D2) of both AAA-peroxins is essential for their function. The conserved D2-domains of Pex1p and Pex6p require hydrolysis of ATP for their function in peroxisome biogenesis, indicating that they may providethe driving force for conformational changes triggered by the AAA-peroxins
additional information
structure-function analysis. The D1 of Pex6p does not contain a functional Walker B motif for ATP hydrolysis. AAA-peroxins defective in ATP-hydrolysis of D1 are at least partially functional. In contrast, ATP-hydrolysis of the conserved AAA-domains (D2) of both AAA-peroxins is essential for their function. The conserved D2-domains of Pex1p and Pex6p require hydrolysis of ATP for their function in peroxisome biogenesis, indicating that they may providethe driving force for conformational changes triggered by the AAA-peroxins
additional information
the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789). The ATPase domain in Lon proteases is required for ATP?dependent unfolding of the target protein, prior to degradation by the protease domain
additional information
-
the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789). The ATPase domain in Lon proteases is required for ATP?dependent unfolding of the target protein, prior to degradation by the protease domain
additional information
the murine Pex1p N-terminal domain lacks hydrophobic amino acids. Structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
the murine Pex1p N-terminal domain lacks hydrophobic amino acids. Structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
within the Pex1/Pex6 complex, only the D2 ATPase ring hydrolyzes ATP, while nucleotide binding in the D1 ring promotes complex assembly. ATP hydrolysis by Pex1 is highly coordinated with that of Pex6
additional information
within the Pex1/Pex6 complex, only the D2 ATPase ring hydrolyzes ATP, while nucleotide binding in the D1 ring promotes complex assembly. ATP hydrolysis by Pex1 is highly coordinated with that of Pex6
additional information
-
within the Pex1/Pex6 complex, only the D2 ATPase ring hydrolyzes ATP, while nucleotide binding in the D1 ring promotes complex assembly. ATP hydrolysis by Pex1 is highly coordinated with that of Pex6
additional information
yeast Pex1/6 complex structure analysis, structural insights into inter-domain communication of these unique heterohexameric AAA+ assemblies. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs. The Pex1/6 complex assembles in the presence of a nucleotide, ATP or ATPgammaS, structure modeling, overview
additional information
yeast Pex1/6 complex structure analysis, structural insights into inter-domain communication of these unique heterohexameric AAA+ assemblies. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs. The Pex1/6 complex assembles in the presence of a nucleotide, ATP or ATPgammaS, structure modeling, overview
additional information
-
yeast Pex1/6 complex structure analysis, structural insights into inter-domain communication of these unique heterohexameric AAA+ assemblies. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs. The Pex1/6 complex assembles in the presence of a nucleotide, ATP or ATPgammaS, structure modeling, overview
additional information
-
molecular structure modeling
-
additional information
-
the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789). The ATPase domain in Lon proteases is required for ATP?dependent unfolding of the target protein, prior to degradation by the protease domain
-
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oligomer
-
homo-oligomer in the cytosol, hetero-oligomer on peroxisome membranes
?
-
x * 104000, PEX6, SDS-PAGE
?
-
x * 141000, PEX1, SDS-PAGE
?
-
x * 110000, Pex6p, SDS-PAGE
?
-
x * 120000, Pex1p, SDS-PAGE
heptamer
-
7 * 147000, small-angle X-ray scattering, SAXS, analysis
heptamer
-
7 * 147000, small-angle X-ray scattering, SAXS, analysis
-
heterohexamer
Q9FNP1; Q8RY16
-
heterohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, Pex1p/Pex6p forms a type II heterohexameric complex with two AAA+ rings (D1 ring, D2 ring) and large N-terminal domains positioned on top and aside of the double ring structure
heterohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, Pex1p/Pex6p forms a type II heterohexameric complex with two AAA+ rings (D1 ring, D2 ring) and large N-terminal domains positioned on top and aside of the double ring structure
heterohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, Pex1p/Pex6p forms a type II heterohexameric complex with two AAA+ rings (D1 ring, D2 ring) and large N-terminal domains positioned on top and aside of the double ring structure
heterohexamer
Pex1p and Pex6p interact and form a heterohexameric complex in a one-to-one ratio of both AAA-proteins
heterohexamer
the enzyme complex exhibts a unique double-ring structure, cryo-electron microscopy
heterohexamer
the Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits, structure analysis, overview
heterohexamer
trimers of dimers, the peroxisomal proteins Pex1 and Pex6 form a heterohexameric type II AAA+ ATPase complex. The heterohexamer forms a trimer of Pex1/6 dimers with a triangular geometry that is atypical for AAA+ complexes. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs
heterohexamer
-
Pex1 and Pex6 form a single, heterohexameric type-2 AAA-ATPase motor
heterohexamer
-
Pex1 and Pex6 forma heterohexamer composed of a trimer of Pex1/6 dimers
heterohexamer
-
the ATPases Pex1p and Pex6p represent a heterohexameric enzyme complex
homohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, the enzyme combines its AAA+ ring with a C-terminal protease segment
homohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, the enzyme combines its AAA+ ring with a C-terminal protease segment
homohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, the enzyme combines its AAA+ ring with a C-terminal protease segment
homohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, the enzyme combines its AAA+ ring with a C-terminal protease segment
additional information
-
Pex1p and Pex6p are believed to form heterohexameric structures
additional information
since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins. Under ATP depletion, Pex6p remains at the peroxisomal membrane, whereas Pex1p is released to the cytosol, probably as homotrimeric version
additional information
since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins. Under ATP depletion, Pex6p remains at the peroxisomal membrane, whereas Pex1p is released to the cytosol, probably as homotrimeric version
additional information
since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins
additional information
since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins
additional information
the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789)
additional information
-
the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789)
additional information
-
the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789)
-
additional information
-
Pex1p and Pex6p are believed to form heterohexameric structures
additional information
when the yeast Pex1p-Pex6p complex disassembles under ATP depleting conditions, Pex1p adopts a homotrimeric conformation, while Pex6p is monomeric. Since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins
additional information
when the yeast Pex1p-Pex6p complex disassembles under ATP depleting conditions, Pex1p adopts a homotrimeric conformation, while Pex6p is monomeric. Since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins
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Q144stop
naturally occuring mutation, gene At5g47040 expression is sufficient to rescue the apem10 phenotype, overview
D662N
-
Walker-motif mutant: mutant shows a lower level of targeting to EGFP-Pex26p as compared to wild-type
D803N
-
Walker-motif mutant: mutant is transported to peroxisomes by EGFP-Pex26p to the same level as wild-type
D940N
-
Walker-motif mutant: mutant shows a normal or slightly increased level of targeting to EGFP-Pex26p as compared to wild-type
K476E
-
Walker-motif mutant: mutant shows a lower level of targeting to EGFP-Pex26p as compared to wild-type
K605E
-
Walker-motif mutant: mutant are significantly reduced in translocation to EGFP-Pex26p as compared to wild-type
K750E
-
Walker-motif mutant: mutant shows a lower level of targeting to EGFP-Pex26p as compared to wild-type
K887E
-
Walker-motif mutant: mutant are significantly reduced in translocation to EGFP-Pex26p as compared to wild-type
L664P
-
mutation identified in patients with Zellweger syndrome, stable protein, but verly low interaction with Pex6 protein
K174A
-
mutant, binds with approximately the same affinity and specificity as the wild-type protein
R135A
-
mutant, the conserved arginine surrounded by hydrophobic residues is essential for lipid binding
T246A
-
the mutation of the Pex6 peptide decreases the apparent affinity of Pex1/Pex6 for Pex15 from 0.0006 to 0.002 mM
V245A
-
the mutation of the Pex6 peptide decreases the apparent affinity of Pex1/Pex6 for Pex15 from 0.0006 to 0.002 mM
G843D
-
most frequently identified mutation in patients with infantile Refsum disease, protein is rapidly degraded in vivo at 37°C, interaction with Pex6 protein at 50% of wild-type level
G843D
-
the mutation of the PEX1 component causes a mild form of peroxisome biogenesis disorder
S815A
-
site-directed mutagensis, a single amino acid substitution in the conserved catalytic dyad leads to a proteolytically inactive variant Plnin
S815A
-
site-directed mutagensis, a single amino acid substitution in the conserved catalytic dyad leads to a proteolytically inactive variant Plnin
-
additional information
-
use of the mutants pex6-1 and pex6-1(35S-PEX5) which has decreased resp. elevated PEX5 levels
additional information
-
deletion mutant of residues 634-690, identified in patients with Zellweger syndrome, stable protein, but verly low interaction with Pex6 protein
additional information
construction of the various disruption strains of the Hansenula polymorpha PLN gene, the pln deletion cells grow normally like wild-type cells on methanol at 37°C. Growth is also unaffected at elevated growth temperatures (45°C) or upon heat shock
additional information
-
construction of the various disruption strains of the Hansenula polymorpha PLN gene, the pln deletion cells grow normally like wild-type cells on methanol at 37°C. Growth is also unaffected at elevated growth temperatures (45°C) or upon heat shock
additional information
-
construction of the various disruption strains of the Hansenula polymorpha PLN gene, the pln deletion cells grow normally like wild-type cells on methanol at 37°C. Growth is also unaffected at elevated growth temperatures (45°C) or upon heat shock
-
additional information
a mutation of the conserved Walker A lysine in the D1 domain of Pex1, but not Pex6, dramatically affects the recovery of fully assembled recombinant hexamer. Compared to the ATPase rate of wild-type Pex1/Pex6, this Pex1 D1 Walker A mutant hexamer retains 70% activity. The Pex1 and Pex6 D2 Walker B double mutant shows no ATP-hydrolysis activity. The ATPase rate of the Pex1-WB/Pex6 mutant is very similar to the rate observed for wild-type Pex1/Pex6 at saturating concentrations of tPex15, but unlike for wild-type Pex1/Pex6, no inhibition of Pex1-WB/Pex6 by tPex15 is observed
additional information
a mutation of the conserved Walker A lysine in the D1 domain of Pex1, but not Pex6, dramatically affects the recovery of fully assembled recombinant hexamer. Compared to the ATPase rate of wild-type Pex1/Pex6, this Pex1 D1 Walker A mutant hexamer retains 70% activity. The Pex1 and Pex6 D2 Walker B double mutant shows no ATP-hydrolysis activity. The ATPase rate of the Pex1-WB/Pex6 mutant is very similar to the rate observed for wild-type Pex1/Pex6 at saturating concentrations of tPex15, but unlike for wild-type Pex1/Pex6, no inhibition of Pex1-WB/Pex6 by tPex15 is observed
additional information
-
a mutation of the conserved Walker A lysine in the D1 domain of Pex1, but not Pex6, dramatically affects the recovery of fully assembled recombinant hexamer. Compared to the ATPase rate of wild-type Pex1/Pex6, this Pex1 D1 Walker A mutant hexamer retains 70% activity. The Pex1 and Pex6 D2 Walker B double mutant shows no ATP-hydrolysis activity. The ATPase rate of the Pex1-WB/Pex6 mutant is very similar to the rate observed for wild-type Pex1/Pex6 at saturating concentrations of tPex15, but unlike for wild-type Pex1/Pex6, no inhibition of Pex1-WB/Pex6 by tPex15 is observed
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Lee, Y.J.; Wickner, R.B.
AFG1, a new member of the SEC18-NSF, PAS1, CDC48-VCP, TBP family of ATPases
Yeast
8
787-790
1992
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Hansenula polymorpha Pex1p and Pex6p are peroxisome-associated AAA proteins that functionally and physically interact
Yeast
15
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Dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p involved in shuttling of the PTS1 receptor Pex5p in peroxisome biogenesis
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Saccharomyces cerevisiae
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Saffert, P.; Enenkel, C.; Wendler, P.
Structure and function of p97 and Pex1/6 type II AAA+ complexes
Front. Mol. Biosci.
4
33
2017
Saccharomyces cerevisiae, Caenorhabditis elegans
brenda
Pedrosa, A.G.; Francisco, T.; Ferreira, M.J.; Rodrigues, T.A.; Barros-Barbosa, A.; Azevedo, J.E.
A mechanistic perspective on PEX1 and PEX6, two AAA+ proteins of the peroxisomal protein import machinery
Int. J. Mol. Sci.
20
5246
2019
Saccharomyces cerevisiae
brenda
Pedrosa, A.G.; Francisco, T.; Bicho, D.; Dias, A.F.; Barros-Barbosa, A.; Hagmann, V.; Dodt, G.; Rodrigues, T.A.; Azevedo, J.E.
Peroxisomal monoubiquitinated PEX5 interacts with the AAA ATPases PEX1 and PEX6 and is unfolded during its dislocation into the cytosol
J. Biol. Chem.
293
11553-11563
2018
Homo sapiens
brenda
Schwerter, D.; Grimm, I.; Girzalsky, W.; Erdmann, R.
Receptor recognition by the peroxisomal AAA complex depends on the presence of the ubiquitin moiety and is mediated by Pex1p
J. Biol. Chem.
293
15458-15470
2018
Saccharomyces cerevisiae
brenda
Gardner, B.M.; Castanzo, D.T.; Chowdhury, S.; Stjepanovic, G.; Stefely, M.S.; Hurley, J.H.; Lander, G.C.; Martin, A.
The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading
Nat. Commun.
9
135
2018
Saccharomyces cerevisiae
brenda
Gonzalez, K.L.; Fleming, W.A.; Kao, Y.T.; Wright, Z.J.; Venkova, S.V.; Ventura, M.J.; Bartel, B.
Disparate peroxisome-related defects in Arabidopsis pex6 and pex26 mutants link peroxisomal retrotranslocation and oil body utilization
Plant J.
92
110-128
2017
Arabidopsis thaliana (Q9FNP1 and Q8RY16)
brenda
Grimm, I.; Saffian, D.; Girzalsky, W.; Erdmann, R.
Nucleotide-dependent assembly of the peroxisomal receptor export complex
Sci. Rep.
6
19838
2016
Saccharomyces cerevisiae
brenda