A role for widely interspaced zinc finger (WIZ) in retention of the G9a methyltransferase on chromatin

Jeremy M. Simon, Joel S. Parker, Feng Liu, Scott B. Rothbart, Slimane Ait-Si-ali, Brian D. Strahl, Jian Jin, Ian J. Davis, Amber L. Mosley, Samantha G. Pattenden

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

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 moleculebased inhibition of G9a/GLP, supporting discrete functions of the G9a-GLP-WIZ chromatin complex in addition to H3K9me2 methylation.

Original languageEnglish (US)
Pages (from-to)26088-26102
Number of pages15
JournalJournal of Biological Chemistry
Volume290
Issue number43
DOIs
StatePublished - Oct 23 2015

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Simon, J. M., Parker, J. S., Liu, F., Rothbart, S. B., Ait-Si-ali, S., Strahl, B. D., Jin, J., Davis, I. J., Mosley, A. L., & Pattenden, S. G. (2015). A role for widely interspaced zinc finger (WIZ) in retention of the G9a methyltransferase on chromatin. Journal of Biological Chemistry, 290(43), 26088-26102. https://doi.org/10.1074/jbc.M115.654459