| Structural highlights
Function
SAS3_YEAST Catalytic component of the NuA3 histone acetyltransferase complex, that acetylates H3K14 (PubMed:10600516, PubMed:10817755, PubMed:11731478, PubMed:16581777, PubMed:17157260, PubMed:25104842). The NuA3 HAT complex has 2 functionally distinct forms. NuA3a binds H3K4me3, through the PHD finger of YNG1, and acetylates H3K14 at the promoter region of actively transcribed genes to promote transcription initiation. NuA3b binds H3K36me3 at the coding regions of actively transcribed genes, through the PWWP domain of PDP3, and coordinates transcription elongation (PubMed:17157260, PubMed:25104842). In vitro, SAS3 acetylates free histones H3 and H4 (PubMed:10600516). It is involved in silencing the HMR locus (PubMed:16581777, PubMed:8782818).[1] [2] [3] [4] [5] [6] [7]
References
- ↑ Takechi S, Nakayama T. Sas3 is a histone acetyltransferase and requires a zinc finger motif. Biochem Biophys Res Commun. 1999 Dec 20;266(2):405-10. PMID:10600516 doi:10.1006/bbrc.1999.1836
- ↑ John S, Howe L, Tafrov ST, Grant PA, Sternglanz R, Workman JL. The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex. Genes Dev. 2000 May 15;14(10):1196-208 PMID:10817755
- ↑ Howe L, Auston D, Grant P, John S, Cook RG, Workman JL, Pillus L. Histone H3 specific acetyltransferases are essential for cell cycle progression. Genes Dev. 2001 Dec 1;15(23):3144-54. PMID:11731478 doi:10.1101/gad.931401
- ↑ Martin DG, Grimes DE, Baetz K, Howe L. Methylation of histone H3 mediates the association of the NuA3 histone acetyltransferase with chromatin. Mol Cell Biol. 2006 Apr;26(8):3018-28. PMID:16581777 doi:10.1128/MCB.26.8.3018-3028.2006
- ↑ Taverna SD, Ilin S, Rogers RS, Tanny JC, Lavender H, Li H, Baker L, Boyle J, Blair LP, Chait BT, Patel DJ, Aitchison JD, Tackett AJ, Allis CD. Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell. 2006 Dec 8;24(5):785-96. PMID:17157260 doi:http://dx.doi.org/10.1016/j.molcel.2006.10.026
- ↑ Gilbert TM, McDaniel SL, Byrum SD, Cades JA, Dancy BC, Wade H, Tackett AJ, Strahl BD, Taverna SD. A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions. Mol Cell Proteomics. 2014 Nov;13(11):2883-95. PMID:25104842 doi:10.1074/mcp.M114.038224
- ↑ Reifsnyder C, Lowell J, Clarke A, Pillus L. Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases. Nat Genet. 1996 Sep;14(1):42-9. PMID:8782818 doi:10.1038/ng0996-42
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