色谱 ›› 2013, Vol. 31 ›› Issue (6): 514-517.DOI: 10.3724/SP.J.1123.2013.01008

• 特别策划:定量蛋白质组学专栏 • 上一篇    下一篇

组蛋白H3赖氨酸27和36位甲基化修饰的鉴定

王国娟1,2, 张锴1,2, 何锡文2, 张玉奎1,2,3   

  1. 1. 南开大学药物化学生物学国家重点实验室, 天津 300071;
    2. 南开大学化学学院, 天津 300071;
    3. 中国科学院大连化学物理研究所, 辽宁 大连 116023
  • 收稿日期:2013-01-05 修回日期:2013-03-11 出版日期:2013-06-28 发布日期:2013-06-06
  • 通讯作者: 张锴
  • 基金资助:

    国家重点基础研究发展计划("973"项目)(2012cb910601);国家自然科学基金项目(21275077).

Identification of methylation at lysine 27 and 36 sites in histone H3

WANG Guojuan1,2, ZHANG Kai1,2, HE Xiwen2, ZHANG Yukui1,2,3   

  1. 1. State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, China;
    2. College of Chemistry, Nankai University, Tianjin 300071, China;
    3. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China
  • Received:2013-01-05 Revised:2013-03-11 Online:2013-06-28 Published:2013-06-06
  • Contact: 10.3724/SP.J.1123.2013.01008

摘要:

采用液相色谱-质谱联用技术结合生物信息学分析手段,研究Hela细胞组蛋白H3赖氨酸(Lysine (K))K27和K36位点带有甲基化和二甲基化修饰的多肽鉴定,通过二级质谱碎片解析和二级碎片丰度分析,对组蛋白H3赖氨酸K27和K36上甲基化和二甲基化修饰进行了鉴定和分析。

关键词: 定量蛋白质组学, 翻译后修饰, 液相色谱, 质谱, 组蛋白

Abstract:

we combined high performance liquid chromatography and tandem mass spectrometry (HPLC-MS/MS) with bioinformatics tools to analyze the isobaric modified peptides which were methylated and dimethylated at either lysine (K) 27 or/and K36 from histone H3. They were identified and dissected through alignment of every fragment ion, and the two modified sites were further analyzed according to their relative intensities of MS/MS spectra.

Key words: histone, liquid chromatography (LC), mass spectrometry (MS), post-translational modifications (PTMs), quantitative proteomics

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