| Literature DB >> 30040183 |
Moritz Carl Völker-Albert1, Andreas Schmidt1, Ignasi Forne1, Axel Imhof1.
Abstract
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.Keywords: chemical derivatization of amino acids; histone modifications; lysine acetylation; lysine methylation; mass spectrometry; tandem MS
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Year: 2018 PMID: 30040183 DOI: 10.1002/cpps.54
Source DB: PubMed Journal: Curr Protoc Protein Sci ISSN: 1934-3655