RRC ID 52119
Author Yamagata K, Kobayashi A.
Title The cysteine-rich domain of TET2 binds preferentially to mono- and dimethylated histone H3K36.
Journal J Biochem
Abstract Missense mutations in Ten-eleven translocation 2 (TET2) gene are frequently found in leukaemia patients. Although mutations span the entire coding region, they tend to cluster in the C-terminal enzymatic domain and a cysteine-rich (CR) domain of unknown function. Herein, we found the CR domain binds chromatin preferentially at the histone H3 tail by recognising H3 lysine 36 mono- and dimethylation (H3K36me1/2). Importantly, missense mutations in the CR domain perturbed TET2 recruitment to the target locus and its enzymatic activities. Our findings identify a novel H3K36me recognition domain and uncover a critical link between histone modification and DNA hydroxylation in leukaemogenesis.
Volume 161(4)
Pages 327-330
Published 2017-4-1
DOI 10.1093/jb/mvx004
PII mvx004
PMID 28130413
PMC PMC5412023
MeSH Binding Sites / genetics Chromatin / metabolism Cysteine / genetics Cysteine / metabolism* DNA-Binding Proteins / chemistry DNA-Binding Proteins / genetics DNA-Binding Proteins / metabolism* HEK293 Cells Histones / chemistry Histones / metabolism* Humans Immunoblotting Lysine / chemistry Lysine / metabolism* Methylation Microscopy, Confocal Models, Molecular Mutation, Missense Protein Binding Protein Domains Proto-Oncogene Proteins / chemistry Proto-Oncogene Proteins / genetics Proto-Oncogene Proteins / metabolism*
IF 2.23
Times Cited 4
Resource
Human and Animal Cells 293T(RCB2202)