Reference - Detail
| 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* Dioxygenases 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 | 2.476 |
| Times Cited | 4 |
| Resource | |
| Human and Animal Cells | 293T(RCB2202) |