Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes

被引:269
作者
Steward, Melissa M.
Lee, Jung-Shin
O'Donovan, Aisling
Wyatt, Matt
Bernstein, Bradley E.
Shilatifard, Ali
机构
[1] St Louis Univ, Sch Med, Dept Biochem, St Louis, MO 63104 USA
[2] Massachusetts Gen Hosp, Dept Pathol, Charlestown, MA 02129 USA
[3] Harvard Univ, Sch Med, Charlestown, MA 02129 USA
[4] St Louis Univ, Sch Med, Ctr Canc, St Louis, MO 63104 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1038/nsmb1131
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
MLL complexes are homologs of yeast COMPASS capable of methylating histone H3 Lys4 (H3K4). ASH2L, RbBP5 and WDR5 are conserved subunits of MLL complexes with homology to the Cps40/Cps60, Cps50 and Cps30 subunits of COMPASS, respectively. We report that ASH2L differentially regulates MLL's catalysis of H3K4 trimethylation similarly to Cps40 and Cps60. Furthermore, WDR5 is required to maintain MLL complex integrity, including the stability of ASH2L within the complex. These findings offer insight into the molecular role of ASH2L, and by extension that of WDR5, in proper H3K4 trimethylation.
引用
收藏
页码:852 / 854
页数:3
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