组蛋白修饰的质谱分析

Q1 Biochemistry, Genetics and Molecular Biology

Current Protocols in Protein Science Pub Date : 2018-04-16 DOI:10.1002/cpps.54

Moritz Carl Völker-Albert, Andreas Schmidt, Ignasi Forne, Axel Imhof

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引用次数: 13

摘要

组蛋白N端经过多种翻译后修饰，显著扩展了遗传密码的信息潜力。此外，这些修饰标记了特定的染色质区域，调节表观遗传控制、谱系承诺和染色体的整体功能。人们普遍认为组蛋白修饰影响染色质功能，但组蛋白尾部修饰和特定修饰组合产生的确切机制，以及它们如何相互串扰，仍然是一个谜。质谱法是分析组蛋白修饰的金标准方法，因为它允许修饰和组合的量化。本单元描述了高分辨率质谱法如何用于研究组蛋白翻译后修饰。©2018 by John Wiley &儿子,Inc。

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Analysis of Histone Modifications by Mass Spectrometry

Histone N termini undergo diverse post-translational modifications that significantly extend the information potential of the genetic code. Moreover, these modifications mark specific chromatin regions, modulating epigenetic control, lineage commitment, and overall function of chromosomes. It is widely accepted that histone modifications affect chromatin function, but the exact mechanisms by which modifications on histone tails and specific combinations of modifications are generated, and how they cross-talk with one another, are still enigmatic. Mass spectrometry is the gold-standard method for analyzing histone modifications, as it allows the quantification of modifications and combinations. This unit describes how high-resolution mass spectrometry can be used to study histone post-translational modifications. © 2018 by John Wiley & Sons, Inc.

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来源期刊

Current Protocols in Protein Science Biochemistry, Genetics and Molecular Biology-Biochemistry

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期刊介绍： With the mapping of the human genome, more and more researchers are exploring protein structures and functions in living organisms. Current Protocols in Protein Science provides protein scientists, biochemists, molecular biologists, geneticists, and others with the first comprehensive suite of protocols for this growing field.