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Progress in Chemistry 2010, Vol. 22 Issue (04): 713-719 Previous Articles   Next Articles

• Invited Article •

Development of Identification for Post-Translational Modifications in Histones by Mass Spectrometry Based Proteomics

Chen Ying1; Zhang Kai1**; He Xiwen1; Zhang Yukui1,2   

  1. (1. Department of Chemistry, Nankai University, Tianjin 300071, China; 2. National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China)
  • Received: Revised: Online: Published:
  • Contact: Zhang Kai E-mail:zhangkai730@yahoo.com.cn
  • Supported by:

    National Natural Science Foundation of China;National Natural Science Foundation of China

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In eukaryotic cells, chromosomal DNA is packaged into a compact structure, chromatin, with the help of four core histones. The fundamental repeating unit of chromatin is the nucleosome, which contains an octamer of core histones, around 147 base pairs of DNA are wrapped. Post-translational modifications (PTMs) in histones are generally considered to be a major group of epigenetic marks. Accordingly because PTMs alter the properties of histones, hence, affect histone structure and function and regulate the gene expression. Therefore, identification of histones PTMs is the key to discover histone codes. At present mass spectrometry has become a powerful analysis tool. Here, we introduced the novel development of the strategies based on mass spectrometry ("bottom up" and "top down") in mapping histone PTMs, fragment dissociation technologies such as CID, ECD and ETD. We also reported the application of mass spectrometry in addressing histone PTMs sites, identifying histone variants and quantifying differential expression of these PTMs in cells.

Contents
1 The strategies and methods of identification for post-translational modifications in histones by mass spectrometry
1.1 The strategy for histone analysis based mass spectrometry
1.2 MS fragmentation
2 The application of mass spectrometry in post-translational modifications in histones
2.1 Identification and characterization of post-translation modifications in histones
2.2 Identification and characterization of histone variants
2.3 Quantification based mass spectrometry for post-translational modifications in histones

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