Premium
TET 3– OGT interaction increases the stability and the presence of OGT in chromatin
Author(s) -
Ito Ryo,
Katsura Shogo,
Shimada Hiroki,
Tsuchiya Hikaru,
Hada Masashi,
Okumura Tomoko,
Sugawara Akira,
Yokoyama Atsushi
Publication year - 2014
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/gtc.12107
Subject(s) - histone , chromatin , biology , acetylation , epigenome , chromatin immunoprecipitation , 5 hydroxymethylcytosine , 5 methylcytosine , histone h3 , dna , epigenetics , function (biology) , dna methylation , microbiology and biotechnology , biochemistry , gene , gene expression , promoter
Gene expression is controlled by alterations in the epigenome, including DNA methylation and histone modification. Recently, it was reported that 5‐methylcytosine (5mC) is converted to 5‐hydroxymethylcytosine (5hmC) by proteins in the ten‐eleven translocation ( TET ) family. This conversion is believed to be part of the mechanism by which methylated DNA is demethylated. Moreover, histones undergo modifications such as phosphorylation and acetylation. In addition, modification with O ‐linked‐ N ‐acetylglucosamine ( O ‐Glc NA c) by O ‐Glc NA c transferase ( OGT ) was recently identified as a novel histone modification. Herein, we focused on TET 3, the regulation of which is still unclear. We attempted to elucidate the mechanism of its regulation by biochemical approaches. First, we conducted mass spectrometric analysis in combination with affinity purification of FLAG – TET 3, which identified OGT as an important partner of TET 3. Co‐immunoprecipitation assays using a series of deletion mutants showed that the C‐terminal H domain of TET 3 was required for its interaction with OGT . Furthermore, we showed that TET 3 is Glc NA cylated by OGT , although the Glc NA cylation did not affect the global hydroxylation of methylcytosine by TET 3. Moreover, we showed that TET 3 enhanced its localization to chromatin through the stabilization of OGT protein. Taken together, we showed a novel function of TET 3 that likely supports the function of OGT .