WRAD: enabler of the SET1-family of H3K4 methyltransferases

Ernst, P., Vakoc, C. R. (May 2012) WRAD: enabler of the SET1-family of H3K4 methyltransferases. Briefings in Functional Genomics, 11 (3). pp. 217-226. ISSN 2041-2649

Abstract

Methylation of histone H3 at lysine 4 (H3K4) is a conserved feature of active chromatin catalyzed by methyltransferases of the SET1-family (SET1A, SET1B, MLL1, MLL2, MLL3 and MLL4 in humans). These enzymes participate in diverse gene regulatory networks with a multitude of known biological functions, including direct involvement in several human disease states. Unlike most lysine methyltransferases, SET1-family enzymes are only fully active in the context of a multi-subunit complex, which includes a protein module comprised of WDR5, RbBP5, ASH2L and DPY-30 (WRAD). These proteins bind in close proximity to the catalytic SET domain of SET1-family enzymes and stimulate H3K4 methyltransferase activity. The mechanism by which WRAD promotes catalysis involves elements of allosteric control and possibly the utilization of a second H3K4 methyltransferase active site present within WRAD itself. WRAD components also engage in physical interactions that recruit SET1-family proteins to target sites on chromatin. Here, the known molecular mechanisms through which WRAD enables the function of SET1-related enzymes will be reviewed.

Item Type:	Paper
Uncontrolled Keywords:	SET1 MLL WDR5 RbBP5 ASH2L DPY-30 lineage leukemia protein-1 homeotic gene-expression trithorax group proteins set-domain protein mll1 core complex histone h3 saccharomyces-cerevisiae molecular regulation structural basis lysine 4
Subjects:	bioinformatics > genomics and proteomics > genetics & nucleic acid processing bioinformatics > genomics and proteomics bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:	Vakoc, Christopher R.
Communities:	CSHL labs > Vakoc lab
Depositing User:	Matt Covey
Date:	May 2012
Date Deposited:	31 Jan 2013 19:47
Last Modified:	31 Jan 2013 19:47
PMCID:	PMC3388306
Related URLs:	Publisher
URI:	https://repository.cshl.edu/id/eprint/26936

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