Histone acetyltransferase

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== Function ==
== Function ==
'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>.
'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>.
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See also [[Histone acetyltransferase 1-2 Complex (HAT1/2)]].
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*'''Histone acetyltransferase P300''' acetylates all 4 core histones in nucleosomes and also non-histone targets.
== Relevance ==
== Relevance ==
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== Structural highlights ==
== Structural highlights ==
<scene name='46/467281/Cv/7'>HAT binds acetyl CoA</scene> in a <scene name='46/467281/Cv/9'>cleft toward the center of the concave surface</scene> of the protein<ref>PMID:9727486</ref>. Water molecules shown as red spheres.
<scene name='46/467281/Cv/7'>HAT binds acetyl CoA</scene> in a <scene name='46/467281/Cv/9'>cleft toward the center of the concave surface</scene> of the protein<ref>PMID:9727486</ref>. Water molecules shown as red spheres.
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</StructureSection>
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== 3D Structures of histone acetyltransferase ==
== 3D Structures of histone acetyltransferase ==
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[[Histone acetyltransferase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Histone acetyltransferase; Human domains – catalytic domain residues 497-662; bromodomain residues 729-837;
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**[[1qso]] - yHAT HPA2 – yeast<br />
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**[[3to7]] – yHAT Esa1<br />
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**[[2rnz]] – yHAT Esa1 chromodomain – NMR
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**[[2ro0]] - yHAT Esa1 knotted Tudor domain – NMR<br />
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**[[1ygh]] – yHAT HAT domain<br />
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**[[1f68]] – hHAT bromodomain (mutant) – human – NMR
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**[[1n72]] - hHAT bromodomain – NMR
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**[[3d7c]] - hHAT bromodomain
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**[[3gg3]] - hHAT PCAF bromodomain
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**[[2ou2]] - hHAT HTATIP<br />
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**[[2eko]] – hHAT HTATIP histone tail-binding domain - NMR
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**[[1z4r]] – hHAT catalytic domain<br />
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**[[3toa]] - hHAT Myst1 residues 177-447<br />
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**[[3tob]] - hHAT Myst1 residues 177-447 (mutant)<br />
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**[[2rc4]] – hHAT Myst3 acetyltransferase domain<br />
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**[[5trm]] - hHAT KAT2A catalytic domain <br />
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**[[4nsq]] - hHAT KAT2B<br />
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**[[4qqg]] - hHAT KAT5 N terminal<br />
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**[[2ln0]] - hHAT KAT6A<br />
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**[[4ljn]] - hHAT KAT6A double PHD finger<br />
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**[[5wci]] - hHAT KAT8 residues 174-449 <br />
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**[[5j8c]], [[5j8f]] - hHAT KAT8 residues 177-447 (mutant)<br />
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**[[2qec]] – HAT HPA2 (mutant) – ''Corynebacterium glutamicum''
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*Histone acetyltransferase binary complexes
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**[[1bob]] – yHAT 1 + acetyl-CoA
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**[[1qsm]] – yHAT HPA2 + acetyl-CoA
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**[[1fy7]], [[1mja]] - yHAT Esa1 + CoA<br />
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**[[3to6]] - yHAT Esa1 + H4 peptide<br />
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**[[4psw]] - yHAT B + H4 peptide<br />
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**[[1e6i]] - yHAT bromodomain + H4 peptide<br />
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**[[1mj9]], [[3to9]] - yHAT Esa1 (mutant) + CoA
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**[[1mjb]] - yHAT Esa1 (mutant) + acetyl-CoA
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**[[3qm0]] - yHAT RTT109 (mutant) + acetyl-CoA
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**[[3q35]], [[3q66]], [[3q68]] – yHAT RTT109 + vacuolar protein sorting-associated protein 75
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**[[5gcn]] – TtHAT Gcn5 + CoA – ''Tetrahymena thermophila'' - NMR<br />
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**[[1wug]], [[1wum]] – hHAT PCAF + small ligand
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**[[1zs5]] – hHAT bromodomain + inhibitor – NMR
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**[[2ozu]] - hHAT MYST3 catalytic domain + acetyl-CoA
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**[[2p0w]] - hHAT 1 catalytic domain + histone H4 peptide
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**[[2rnw]], [[2rnx]] - hHAT PCAF bromodomain + histone H3 peptide - NMR<br />
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**[[5h84]] - hHAT KAT2A catalytic domain + propionyl CoA<br />
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**[[5h86]] - hHAT KAT2A catalytic domain + butyryl CoA<br />
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**[[5trl]] - hHAT KAT2A catalytic domain + succinyl CoA<br />
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**[[5mlj]] - hHAT KAT2A bromodomain + inhibitor<br />
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**[[5lvq]], [[5lvr]], [[5fdz]], [[5fe0]], [[5fe1]], [[5fe2]], [[5fe3]], [[5fe4]], [[5fe5]], [[5fe6]], [[5fe7]], [[5fe8]], [[5fe9]], [[5mkx]] - hHAT KAT2B bromodomain + inhibitor<br />
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**[[4dnc]] – hHAT KAT8 HAT domain + male-specific lethal 1 homolog<br />
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**[[3v43]], [[4lk9]], [[4lka]], [[4llb]], [[5b75]], [[5b76]], [[5b77]], [[5b78]] - hHAT KAT6A + H3.1 peptide<br />
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**[[5u2j]] - hHAT KAT6B + H3K14BU peptide<br />
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**[[5gk9]] - hHAT KAT7 + BRD1<br />
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**[[5tpx]] - HAT GCN5 + probe – ''Plasmodium falciparum''<br />
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**[[5ml0]] - HAT KAT2B bromodomain + inhibitor - mouse<br />
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*Histone acetyltransferase ternary complexes
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**[[3q33]] – yHAT RTT109 + vacuolar protein sorting-associated protein 75 + histone H3 peptide<br />
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**[[4psx]] - yHAT B + H3 peptide + H4 peptide<br />
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**[[5j9q]], [[5j9t]], [[5j9u]], [[5j9w]] - yHAT Esa1 (mutant) + chromatin modification-related protein + enhancer of polycomb-like protein<br />
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**[[1q2c]] - TtHAT Gcn5 + CoA + histone H4 peptide
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**[[1q2d]] - TtHAT Gcn5 + CoA + p53 peptide
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* Histone acetyltransferase P300; domains – core domain residues 1043-1519; bromodomain residues 1040-1161; acetyltransferase domain residues 1287-1664; TAZ2 domain 1723-1836:
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**[[3i3j]] – hHAT P300 bromodomain <br />
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**[[3io2]] – hHAT P300 TAZ2 domain <br />
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**[[4bhw]] - hHAT P300 core (mutant)<br />
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**[[2mh0]] - hHAT P300 TAZ2 + transcription factor ITF-1<br />
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**[[2mh0]], [[2k8f]] - hHAT P300 TAZ2 (mutant) + p53 peptide<br />
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**[[4pzr]], [[4pzs]] - hHAT P300 acetyltransferase domain residues 1287-1664 (mutant) + acetyl CoA<br />
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**[[4pzt]] - hHAT P300 acetyltransferase domain (mutant) + acetonyl CoA<br />
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**[[5lkt]] - hHAT P300 residues 1581-1666 + butyryl CoA<br />
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**[[5lku]] - hHAT P300 core + CoA<br />
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**[[5lkx]] - hHAT P300 core (mutant) + propionyl CoA<br />
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**[[5lkz]] - hHAT P300 core (mutant) + crotonyl CoA<br />
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**[[3biy]] – hHAT P300 acetyltransferase domain residues 1287-1666 + lysine CoA derivative<br />
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**[[5bt3]], [[5nu5]], [[5lpk]], [[5lpm]] - hHAT P300 bromodomain + inhibitor<br />
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**[[3p57]] - hHAT P300 TAZ2 domain + myocyte-specific enhancer factor 2A + DNA
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Yeast histone acetyltransferase complex with acetyl CoA and Ca+2 ion (green) (PDB entry 1bob)

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References

  1. ↑ Roth SY, Denu JM, Allis CD. Histone acetyltransferases. Annu Rev Biochem. 2001;70:81-120. PMID:11395403 doi:10.1146/annurev.biochem.70.1.81
  2. ↑ Dekker FJ, van den Bosch T, Martin NI. Small molecule inhibitors of histone acetyltransferases and deacetylases are potential drugs for inflammatory diseases. Drug Discov Today. 2014 May;19(5):654-60. doi: 10.1016/j.drudis.2013.11.012. Epub, 2013 Nov 21. PMID:24269836 doi:http://dx.doi.org/10.1016/j.drudis.2013.11.012
  3. ↑ Van Beekum O, Kalkhoven E. Aberrant forms of histone acetyltransferases in human disease. Subcell Biochem. 2007;41:233-62. PMID:17484131
  4. ↑ Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell. 1998 Aug 21;94(4):427-38. PMID:9727486

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Michal Harel, Alexander Berchansky

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