Mapping post-translational modifications of histones H2A, H2B and H4 in Schizosaccharomyces pombe

被引:5
|
作者
Xiong, Lei [1 ]
Wang, Yinsheng [1 ]
机构
[1] Univ Calif Riverside, Dept Chem, Riverside, CA 92521 USA
基金
美国国家卫生研究院;
关键词
Post-translational modification; Yeast; Histone; Mass spectrometry; MASS-SPECTROMETRY; DNA METHYLATION; ACETYLATION; CHROMATIN; RECRUITMENT; PEPTIDES; PATTERNS; H3; DIFFERENTIATION; HETEROCHROMATIN;
D O I
10.1016/j.ijms.2010.08.015
中图分类号
O64 [物理化学(理论化学)、化学物理学]; O56 [分子物理学、原子物理学];
学科分类号
070203 ; 070304 ; 081704 ; 1406 ;
摘要
Core histones are known to carry a variety of post-translational modifications (PTMs), including acetylation, phosphorylation, methylation and ubiquitination, which play important roles in the epigenetic control of gene expression. The nature and biological functions of these PTMs in histones from plants, animals and budding yeast have been extensively investigated. In contrast, the corresponding studies for fission yeast were mainly focused on histone H3. In the present study, we applied LC-nano-ESI-MS/MS, coupled with multiple protease digestion, to identify PTMs in histones H2A, H2B and H4 from Schizosaccharomyces pombe, the typical model organism of fission yeast. Various protease digestions provided high sequence coverage for PTM mapping, and accurate mass measurement of fragment ions allowed for unambiguous differentiation of acetylation from tri-methylation. Many modification sites conserved in other organisms were identified in S. pombe. In addition, some unique modification sites, including N-terminal acetylation in H2A and H2B as well as K123 acetylation in H2A.beta, were observed. Our results provide a comprehensive picture of the PTMs of histones H2A, H2B and H4 in S. pombe, which serves as a foundation for future investigations on the regulation and functions of histone modifications in this important model organism. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码:159 / 165
页数:7
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