Quantitative mass spectrometry reveals the epigenome as a target of arsenic

被引：26
作者：
Chu, Feixia [1 ]
Ren, Xuefeng [2 ]
Chasse, Amanda [1 ]
Hickman, Taylor [1 ]
Zhang, Luoping [2 ]
Yuh, Jessica [2 ]
Smith, Martyn T. [2 ]
Burlingame, Alma L. [3 ]
机构：
[1] Univ New Hampshire, Dept Mol Cellular & Biomed Sci, Durham, NH 03824 USA
[2] Univ Calif Berkeley, Sch Publ Hlth, Superfund Res Program, Berkeley, CA 94720 USA
[3] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94158 USA
来源：
CHEMICO-BIOLOGICAL INTERACTIONS | 2011年 / 192卷 / 1-2期
关键词：
Histone modifications; Mass spectrometry; Quantitation; Arsenic toxicity; Histone acetyltransferase; INDUCED MALIGNANT-TRANSFORMATION; HISTONE H3; POSTTRANSLATIONAL MODIFICATIONS; EPIGENETIC REGULATION; HUMAN-CELLS; PHD FINGER; ACETYLATION; CHROMATIN; PROTEIN; VERNALIZATION;
D O I：
10.1016/j.cbi.2010.11.003
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Recent studies reveal that posttranslational modifications on chromatin proteins, especially histones, organize genomic DNA and mediate various cellular responses to environmental influences. Quantitative mass spectrometric analysis is a powerful approach to reveal these dynamic events on chromatin in a systematic manner. Here, the effects of arsenic exposure on histone epigenetic state were investigated in human UROtsa cells, and a reduction in acetylation level on several histone H3 and H4 lysine residues was detected. Furthermore, MYST1 was shown to be the major histone acetyltransferase for H4 Lys16 and protect UROtsa cells from arsenic toxicity. (C) 2010 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码：113 / 117
页数：5
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