Genomics

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A role for Widely Interspaced Zinc finger (WIZ) in retention of the G9a methyltransferase on chromatin


ABSTRACT: G9a and GLP lysine methyltransferases form a heterodimeric complex that is responsible for the bulk of cellular mono- and di-methylation on histone H3 lysine 9 (H3K9me1/me2). Widely Interspaced Zinc finger (WIZ) associates with the G9a/GLP protein complex, but its role in lysine methylation is poorly defined. Here, we show that WIZ regulates global H3K9me2 levels through a mechanism that involves retention of G9a on chromatin. We also show that WIZ-mediated chromatin loss of G9a/GLP results in altered gene expression and protein-protein interactions that are distinguishable from that of using a molecule-induced enzymatic inhibitor towards G9a/GLP – thus providing evidence that the G9a/GLP/WIZ complex has unique functions when bound to chromatin that are independent of the H3K9me2 mark DMSO, UNC0638, NS, and siWIZ treatments to HEK293T cells, assessing G9a and H3K9me2 localization, each performed in duplicate, plus one input control for each cell condition. 30 samples total.

ORGANISM(S): Homo sapiens  

SUBMITTER: Ian Davis   Jeremy M Simon  Joel S Parker  Samantha G Pattenden 

PROVIDER: E-GEOD-67317 | ArrayExpress | 2015-09-03

SECONDARY ACCESSION(S): SRP056703GSE67317PRJNA279892

REPOSITORIES: GEO, ArrayExpress, ENA

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