the dimer interface includes a domain swapping where strand beta7 of subunit A is located between strands beta5 and beta6 of subunit B, forming an antiparallel beta-sheet
the dimer interface includes a domain swapping where strand beta7 of subunit A is located between strands beta5 and beta6 of subunit B, forming an antiparallel beta-sheet
the dimer interface includes a domain swapping where strand beta7 of subunit A is located between strands beta5 and beta6 of subunit B, forming an antiparallel beta-sheet
the dimer interface includes a domain swapping where strand beta7 of subunit A is located between strands beta5 and beta6 of subunit B, forming an antiparallel beta-sheet
the dimer interface includes a domain swapping where strand beta7 of subunit A is located between strands beta5 and beta6 of subunit B, forming an antiparallel beta-sheet
the dimer interface includes a domain swapping where strand beta7 of subunit A is located between strands beta5 and beta6 of subunit B, forming an antiparallel beta-sheet
the dimer interface includes a domain swapping where strand beta7 of subunit A is located between strands beta5 and beta6 of subunit B, forming an antiparallel beta-sheet
the dimer interface includes a domain swapping where strand beta7 of subunit A is located between strands beta5 and beta6 of subunit B, forming an antiparallel beta-sheet
the NuA4 histone acetyltransferase complex is composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, SWC4, TRA1, VID21, YAF9 and YNG2 subunits
the NuA4 histone acetyltransferase complex is composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, SWC4, TRA1, VID21, YAF9 and YNG2 subunits
isoform IDM1 is predicted to have a metal-binding domain, a plant homeo finger domain and an N-acetyltransferase domain. The plant homeo finger of IDM1 specifically binds the N-terminal tail of histone H3 and the binding is inhibited by H3K4 di- or trimethylation
ability of HATs to form distinct multi-subunit complexes. The human NuA4 complex contains Tip60, but also ATM, a DNA damage related kinase. HAT interacting partners appear to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex
besides the male-specific lethal, MSL, HAT complex, MOF is also a component of the second HAT complex, designated the non-specific lethal, NSL complex, subunit composition of the NSL complex, overview. Two of its subunits,WD repeat domain 5, WDR5, and host cell factor 1, HCF1, are shared with members of the MLL/SET family of histone H3 lysine 4 methyltransferase complexes, and a third subunit, MCRS1, is shared with the human INO80 chromatin-remodeling complex
besides the male-specific lethal, MSL, HAT complex, MOF is also a component of the second HAT complex, designated the non-specific lethal, NSL complex, subunit composition of the NSL complex, overview. Two of its subunits,WD repeat domain 5, WDR5, and host cell factor 1, HCF1, are shared with members of the MLL/SET family of histone H3 lysine 4 methyltransferase complexes, and a third subunit, MCRS1, is shared with the human INO80 chromatin-remodeling complex
enzyme is the catalytic subunit of the male-specific lethal hiostone acetyltransferase complex NSL, which is composed of nine subunits. Two of its subunits,WD-repeat domain WDR5 and host cell factor HCF1, are shared with members of the MLL/SET family of histone H3 lysine 4 methyltransferase complexes, and a third subunit, MCRS1, is shared with the human INO80 chromatin-remodeling complex. Assembly of the enzyme into MSL or NSL complexes controls its substrate specificity
enzyme is the catalytic subunit of the male-specific lethal hiostone acetyltransferase complex NSL, which is composed of nine subunits. Two of its subunits,WD-repeat domain WDR5 and host cell factor HCF1, are shared with members of the MLL/SET family of histone H3 lysine 4 methyltransferase complexes, and a third subunit, MCRS1, is shared with the human INO80 chromatin-remodeling complex. Assembly of the enzyme into MSL or NSL complexes controls its substrate specificity
high mobility group domain-containing protein And-1 forms a complex with both histone H3 and isoform Gcn5. Downregulation of And-1 results in Gcn5 degradation, leading to the reduction of histone H3K9 and H3K56 acetylation. And-1 overexpression stabilizes Gcn5 through protein-protein interactions in vivo
HBO1 consists of the N-terminal domain (NTD) and the conserved C-terminal MYST domain. The NTD of HBO1 consists of a number of loops and a small part of the helix. The structure is highly flexible, which may provide abundant conformation changes for HBO1 activity regulation or protein binding. The MYST domain of HBO1 contains two typical sites for molecule binding, the acetyl-CoA-binding site and histone tail binding site
size-exclusion analysis reveals that most recombinant hARD1/NAA10 form oligomers over time, resulting in the loss of KAT activity. After purification, rhARD1/NAA10 mainly exists in a high oligomeric state and has only a few monomers. The NAT activity is highest for the monomeric enzyme, about 2fold higher compared to the oligomeric enzyme and about 20% higher compared to the dimeric enzyme
size-exclusion analysis reveals that most recombinant hARD1/NAA10 form oligomers over time, resulting in the loss of KAT activity. After purification, rhARD1/NAA10 mainly exists in a high oligomeric state and has only a few monomers. The NAT activity is highest for the monomeric enzyme, about 2fold higher compared to the oligomeric enzyme and about 20% higher compared to the dimeric enzyme
the oligomeric recombinant hARD1/NAA10 loses the ability for lysine acetylation, while the monomeric form clearly shows lysine acetylation activity in vitro
the oligomeric recombinant hARD1/NAA10 loses the ability for lysine acetylation, while the monomeric form clearly shows lysine acetylation activity in vitro
histone acetyltransferase CLOCK forms complexes containing the TBP component of transcription complex TFIID and forms complexes with infected cell proteins ICP4, ICP27, and ICP22. Interactions with TBP and ICP4 occur at relatively late times after infection
NCOAT contains a motif similar to the histone binding domain in the MYST family of HATs, a zinc finger-like motif responsible for substrate recognition
MOZ encodes a large multidomain protein that contains, among others, 2 domains shown to interact with the transcription factor Runx1, a C4H3 domain also referred to as plant homeodomain, an atypical Cys(2)-His-Cys (C2HC) zinc finger domain with a putative nucleosome-binding activity, and a region with homology to the active acetyl-CoA binding site of several HAT proteins
HBO1 consists of the N-terminal domain (NTD) and the conserved C-terminal MYST domain. The NTD of HBO1 consists of a number of loops and a small part of the helix. The structure is highly flexible, which may provide abundant conformation changes for HBO1 activity regulation or protein binding. The MYST domain of HBO1 contains two typical sites for molecule binding, the acetyl-CoA-binding site and histone tail binding site
MOZ encodes a large multidomain protein that contains, among others, 2 domains shown to interact with the transcription factor Runx1, a C4H3 domain also referred to as plant homeodomain, an atypical Cys(2)-His-Cys (C2HC) zinc finger domain with a putative nucleosome-binding activity, and a region with homology to the active acetyl-CoA binding site of several HAT proteins
ability of HATs to form distinct multi-subunit complexes. The SAGA complex contains the histone ubiquitin protease Ubp8 and the histone acetyltransferase Gcn5
NuA4 is a multi-subunit complex, composed of the essential catalytic subunit Esa1, five other essential subunits Act1, Arp4, Epl1, Swc4, Tra1, and seven non-essential subunits Eaf1, Eaf3, Eaf5, Eaf6, Eaf7, Yaf9, and Yng2. Molecular and structural dissection has revealed NuA4 to be modular in nature, assembly of its multiple sub-complexes depends on the Eaf1 subunit
NuA4 is a multi-subunit complex, composed of the essential catalytic subunit Esa1, five other essential subunits Act1, Arp4, Epl1, Swc4, Tra1, and seven non-essential subunits Eaf1, Eaf3, Eaf5, Eaf6, Eaf7, Yaf9, and Yng2. Molecular and structural dissection has revealed NuA4 to be modular in nature, assembly of its multiple sub-complexes depends on the Eaf1 subunit
NuA4 is a multi-subunit complex, composed of the essential catalytic subunit Esa1, five other essential subunits Act1, Arp4, Epl1, Swc4, Tra1, and seven non-essential subunits Eaf1, Eaf3, Eaf5, Eaf6, Eaf7, Yaf9, and Yng2. Molecular and structural dissection has revealed NuA4 to be modular in nature, assembly of its multiple sub-complexes depends on the Eaf1 subunit
tGCN5 is comprised of five alpha-helices and six beta-strands, with N-terminal and C-terminal regions separated by a deep hydrophobic cleft, structure, overview. Phe125 and Phe164 interact with the substrate, but are not directly involved in the acetylation reaction, while residues Glu122, Val123 and Tyr160 are critical for catalysis