| Structural highlights
Function
SET2_YEAST Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent.[1] [2] [3] [4] [5] [6] [7]
Publication Abstract from PubMed
Two new NMR structures of WW domains, the mouse formin binding protein and a putative 84.5 kDa protein from Saccharomyces cerevisiae, show that this domain, only 35 amino acids in length, defines the smallest monomeric triple-stranded antiparallel beta-sheet protein domain that is stable in the absence of disulfide bonds, tightly bound ions or ligands. The structural roles of conserved residues have been studied using site-directed mutagenesis of both wild type domains. Crucial interactions responsible for the stability of the WW structure have been identified. Based on a network of highly conserved long range interactions across the beta-sheet structure that supports the WW fold and on a systematic analysis of conserved residues in the WW family, we have designed a folded prototype WW sequence.
Structural analysis of WW domains and design of a WW prototype.,Macias MJ, Gervais V, Civera C, Oschkinat H Nat Struct Biol. 2000 May;7(5):375-9. PMID:10802733[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Strahl BD, Grant PA, Briggs SD, Sun ZW, Bone JR, Caldwell JA, Mollah S, Cook RG, Shabanowitz J, Hunt DF, Allis CD. Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression. Mol Cell Biol. 2002 Mar;22(5):1298-306. PMID:11839797
- ↑ Xiao T, Hall H, Kizer KO, Shibata Y, Hall MC, Borchers CH, Strahl BD. Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast. Genes Dev. 2003 Mar 1;17(5):654-63. PMID:12629047 doi:https://dx.doi.org/10.1101/gad.1055503
- ↑ Schaft D, Roguev A, Kotovic KM, Shevchenko A, Sarov M, Shevchenko A, Neugebauer KM, Stewart AF. The histone 3 lysine 36 methyltransferase, SET2, is involved in transcriptional elongation. Nucleic Acids Res. 2003 May 15;31(10):2475-82. doi: 10.1093/nar/gkg372. PMID:12736296 doi:https://dx.doi.org/10.1093/nar/gkg372
- ↑ Krogan NJ, Kim M, Tong A, Golshani A, Cagney G, Canadien V, Richards DP, Beattie BK, Emili A, Boone C, Shilatifard A, Buratowski S, Greenblatt J. Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II. Mol Cell Biol. 2003 Jun;23(12):4207-18. doi: 10.1128/MCB.23.12.4207-4218.2003. PMID:12773564 doi:https://dx.doi.org/10.1128/MCB.23.12.4207-4218.2003
- ↑ Landry J, Sutton A, Hesman T, Min J, Xu RM, Johnston M, Sternglanz R. Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae. Mol Cell Biol. 2003 Sep;23(17):5972-8. doi: 10.1128/MCB.23.17.5972-5978.2003. PMID:12917322 doi:https://dx.doi.org/10.1128/MCB.23.17.5972-5978.2003
- ↑ Kizer KO, Phatnani HP, Shibata Y, Hall H, Greenleaf AL, Strahl BD. A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation. Mol Cell Biol. 2005 Apr;25(8):3305-16. PMID:15798214 doi:https://dx.doi.org/25/8/3305
- ↑ Rao B, Shibata Y, Strahl BD, Lieb JD. Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide. Mol Cell Biol. 2005 Nov;25(21):9447-59. PMID:16227595 doi:https://dx.doi.org/25/21/9447
- ↑ Macias MJ, Gervais V, Civera C, Oschkinat H. Structural analysis of WW domains and design of a WW prototype. Nat Struct Biol. 2000 May;7(5):375-9. PMID:10802733 doi:10.1038/75144
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