Structure of the SPRY domain of human Ash2L and its interactions with RbBP5 and DPY30
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/cr20129.pdf
Reference10 articles.
1. Ruthenburg AJ, Allis CD, Wysocka J . Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. Molecular cell 2007; 25:15–30.
2. Dou Y, Milne TA, Ruthenburg AJ, et al. Regulation of MLL1 H3K4 methyltransferase activity by its core components. Nat Struct Mol Biol 2006; 13:713–719.
3. Steward MM, Lee JS, O'Donovan A, Wyatt M, Bernstein BE, Shilatifard A . Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes. Nat Struct Mol Biol 2006; 13:852–854.
4. Cho YW, Hong T, Hong S, et al. PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J Biol Chem 2007; 282:20395–20406.
5. Cao F, Chen Y, Cierpicki T, et al. An Ash2L/RbBP5 heterodimer stimulates the MLL1 methyltransferase activity through coordinated substrate interactions with the MLL1 SET domain. PLoS One 2010; 5:e14102.
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