TRIM66 reads unmodified H3R2K4 and H3K56ac to respond to DNA damage in embryonic stem cells

TRIM66 reads unmodified H3R2K4 and H3K56ac to respond to DNA damage in embryonic stem cells

TRIM66 protein has an N-terminal tripartite motif and a C-terminal PHD Bromodomain. Here the authors show the specific histone modification recognition of TRIM66-PHD-Bromodomain through crystallography and biochemistry assay, and further reveal that TRIM66 recognition of certain histone modification...

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Autores principales: Jiajing Chen, Zikang Wang, Xudong Guo, Fudong Li, Qingtao Wei, Xuwen Chen, Deshun Gong, Yanxin Xu, Wen Chen, Yongrui Liu, Jiuhong Kang, Yunyu Shi
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/9268d15d68b845c18555dcf38329e88d
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spelling oai:doaj.org-article:9268d15d68b845c18555dcf38329e88d2021-12-02T15:35:53ZTRIM66 reads unmodified H3R2K4 and H3K56ac to respond to DNA damage in embryonic stem cells10.1038/s41467-019-12126-42041-1723https://doaj.org/article/9268d15d68b845c18555dcf38329e88d2019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12126-4https://doaj.org/toc/2041-1723TRIM66 protein has an N-terminal tripartite motif and a C-terminal PHD Bromodomain. Here the authors show the specific histone modification recognition of TRIM66-PHD-Bromodomain through crystallography and biochemistry assay, and further reveal that TRIM66 recognition of certain histone modification is important for DNA damage repair in ESCs.Jiajing ChenZikang WangXudong GuoFudong LiQingtao WeiXuwen ChenDeshun GongYanxin XuWen ChenYongrui LiuJiuhong KangYunyu ShiNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-17 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Jiajing Chen
Zikang Wang
Xudong Guo
Fudong Li
Qingtao Wei
Xuwen Chen
Deshun Gong
Yanxin Xu
Wen Chen
Yongrui Liu
Jiuhong Kang
Yunyu Shi
TRIM66 reads unmodified H3R2K4 and H3K56ac to respond to DNA damage in embryonic stem cells
description TRIM66 protein has an N-terminal tripartite motif and a C-terminal PHD Bromodomain. Here the authors show the specific histone modification recognition of TRIM66-PHD-Bromodomain through crystallography and biochemistry assay, and further reveal that TRIM66 recognition of certain histone modification is important for DNA damage repair in ESCs.
format article
author Jiajing Chen
Zikang Wang
Xudong Guo
Fudong Li
Qingtao Wei
Xuwen Chen
Deshun Gong
Yanxin Xu
Wen Chen
Yongrui Liu
Jiuhong Kang
Yunyu Shi
author_facet Jiajing Chen
Zikang Wang
Xudong Guo
Fudong Li
Qingtao Wei
Xuwen Chen
Deshun Gong
Yanxin Xu
Wen Chen
Yongrui Liu
Jiuhong Kang
Yunyu Shi
author_sort Jiajing Chen
title TRIM66 reads unmodified H3R2K4 and H3K56ac to respond to DNA damage in embryonic stem cells
title_short TRIM66 reads unmodified H3R2K4 and H3K56ac to respond to DNA damage in embryonic stem cells
title_full TRIM66 reads unmodified H3R2K4 and H3K56ac to respond to DNA damage in embryonic stem cells
title_fullStr TRIM66 reads unmodified H3R2K4 and H3K56ac to respond to DNA damage in embryonic stem cells
title_full_unstemmed TRIM66 reads unmodified H3R2K4 and H3K56ac to respond to DNA damage in embryonic stem cells
title_sort trim66 reads unmodified h3r2k4 and h3k56ac to respond to dna damage in embryonic stem cells
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/9268d15d68b845c18555dcf38329e88d
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