Tri-methylation of ATF7IP by G9a/GLP recruits the chromodomain protein MPP8.

ABSTRACT:

Background

G9a and the related enzyme GLP were originally identified as histone lysine methyltransferases and then shown to also methylate several other non-histone proteins.

Results

Here, we performed a comprehensive screen to identify their substrates in mouse embryonic stem cells (mESCs). We identified 59 proteins, including histones and other known substrates. One of the identified substrates, activating transcriptional factor 7-interacting protein 1 (ATF7IP), is tri-methylated at a histone H3 lysine 9 (H3K9)-like mimic by the G9a/GLP complex, although this complex mainly introduces di-methylation on H3K9 and DNA ligase 1 (LIG1) K126 in cells. The catalytic domain of G9a showed a higher affinity for di-methylated lysine on ATF7IP than LIG1, which may create different met

SUBMITTER: Tsusaka T 

PROVIDER: S-EPMC6172828 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature