期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 290, 期 43, 页码 26088-26102出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M115.654459
关键词
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资金
- National Institutes of Health [CA181343, R01GM110058, R01CA166447, R01GM103893]
- W. M. Keck Foundation
- National Institutes of Health from NIGMS [R01GM100919]
- Carolina Partnership
- University Cancer Research Fund, University of North Carolina at Chapel Hill
G9a and GLP lysine methyltransferases form a heterodimeric complex that is responsible for the majority of histone H3 lysine 9 mono-and di-methylation (H3K9me1/me2). Widely interspaced zinc finger (WIZ) associates with the G9a-GLP protein complex, but its role in mediating lysine methylation is poorly defined. Here, we show that WIZ regulates global H3K9me2 levels by facilitating the interaction of G9a with chromatin. Disrupting the association of G9a-GLP with chromatin by depleting WIZ resulted in altered gene expression and protein-protein interactions that were distinguishable from that of small molecule-based inhibition of G9a/GLP, supporting discrete functions of the G9a-GLP-WIZ chromatin complex in addition to H3K9me2 methylation.
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