Posttranslational modifications of human histone H3: An update

被引：56
作者：
Xu, Yan-Ming [1 ]
Du, Ji-Ying [1 ]
Lau, Andy T. Y. [1 ]
机构：
[1] Shantou Univ, Coll Med, Dept Cell Biol & Genet, Lab Canc Biol & Epigenet, Shantou 515041, Guangdong, Peoples R China
来源：
PROTEOMICS | 2014年 / 14卷 / 17-18期
基金：
中国国家自然科学基金;
关键词：
Cell biology; Histone H3; Mass spectrometry; Novel posttranslational modifications; Tandem mass spectrometry; ACETYLGLUCOSAMINE O-GLCNAC; ARGININE METHYLATION; SYMMETRIC DIMETHYLATION; COVALENT MODIFICATIONS; CHROMATIN MODIFICATION; THR-3; PHOSPHORYLATION; LYSINE PROPIONYLATION; DNA METHYLATION; DYNAMIC CHANGES; CELL-CYCLE;
D O I：
10.1002/pmic.201300435
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Histone proteins, the fundamental components of chromatin, are highly conserved proteins that present in eukaryotic nuclei. They organize genomic DNA to form nucleosomes, the basic units of chromatin. PTMs of histones play essential roles in many biological processes, such as chromatin condensation, gene expression, cell differentiation, and apoptosis. With the advancement of proteomic technology, a growing number of histone PTMs have been identified, including ADP-ribosylation, biotinylation, citrullination, crotonylation, O-GlcNAcylation, glutathionylation, succinylation, and so on. Because of the fast growing list of these PTMs in just a few years, the functions of these marks are being studied intensively. As histone H3 has the most number of PTMs among the histone members, in this review, we would like to present the overall concepts of the more familiar PTMs as well as discussing all the recently identified yet less well-known PTMs on human histone H3.
引用
收藏
页码：2047 / 2060
页数：14
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