K(lysine) acetyltransferase 8 (KAT8) is an enzyme that in humans is encoded by the KAT8 gene.[5][6]

KAT8
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesKAT8, MOF, MYST1, ZC2HC8, hMOF, lysine acetyltransferase 8, LIGOWS
External IDsOMIM: 609912; MGI: 1915023; HomoloGene: 41676; GeneCards: KAT8; OMA:KAT8 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_032188
NM_182958

NM_026370
NM_001360699

RefSeq (protein)

NP_115564
NP_892003

NP_080646
NP_001347628

Location (UCSC)Chr 16: 31.11 – 31.13 MbChr 7: 127.51 – 127.53 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

edit

The MYST family of histone acetyltransferases, which includes KAT8, was named for the founding members MOZ (MYST3; MIM 601408), yeast YBF2 and SAS2, and TIP60 (HTATIP; MIM 601409). All members of this family contain a MYST region of about 240 amino acids with a canonical acetyl-CoA-binding site and a C2HC-type zinc finger motif. Most MYST proteins also have a chromodomain involved in protein-protein interactions and targeting transcriptional regulators to chromatin.[6]

KAT8 is also known as MOF, and in humans hMOF. Given its fundamental role in modulating higher-order chromatin structure, hMOF is involved in many of the steps of the DNA damage response.[7] The human hMOF gene encodes an enzyme that specifically acetylates histone H4 at lysine 16.[7][8] The depletion of hMOF greatly decreases DNA double-strand break repair by both non-homologous end joining and homologous recombination.[8] Thus MOF activity is critical for double-strand break repair.[8]

Interactions

edit

KAT8 has been shown to interact with MORF4L1.[9]

References

edit
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000103510Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030801Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Neal KC, Pannuti A, Smith ER, Lucchesi JC (Jan 2000). "A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1490 (1–2): 170–4. doi:10.1016/s0167-4781(99)00211-0. PMID 10786633.
  6. ^ a b "Entrez Gene: MYST1 MYST histone acetyltransferase 1".
  7. ^ a b Chen QY, Costa M, Sun H (2015). "Structure and function of histone acetyltransferase MOF". AIMS Biophys. 2 (4): 555–569. doi:10.3934/biophy.2015.4.555. PMC 5425159. PMID 28503659.
  8. ^ a b c Sharma GG, So S, Gupta A, Kumar R, Cayrou C, Avvakumov N, Bhadra U, Pandita RK, Porteus MH, Chen DJ, Cote J, Pandita TK (July 2010). "MOF and histone H4 acetylation at lysine 16 are critical for DNA damage response and double-strand break repair". Mol Cell Biol. 30 (14): 3582–95. doi:10.1128/MCB.01476-09. PMC 2897562. PMID 20479123.
  9. ^ Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM (Dec 2002). "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation". The Journal of Biological Chemistry. 277 (52): 50860–6. doi:10.1074/jbc.M203839200. PMID 12397079.

Further reading

edit
edit
  • Overview of all the structural information available in the PDB for UniProt: Q9H7Z6 (Human Histone acetyltransferase KAT8) at the PDBe-KB.
  • Overview of all the structural information available in the PDB for UniProt: Q9D1P2 (Mouse Histone acetyltransferase KAT8) at the PDBe-KB.