Protein Acetylation

Volume 981 of the series Methods in Molecular Biology pp 1-11


Validation of Protein Acetylation by Mass Spectrometry

  • Barry M. ZeeAffiliated withDepartment of Molecular Biology, Princeton University
  • , Benjamin A. GarciaAffiliated withDepartment of Molecular Biology, Princeton UniversityDepartment of Chemistry, Princeton University

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Due to the key role of posttranslational modifications (PTMs) such as lysine acetylation in numerous signaling and regulatory pathways, the ability to identify novel PTMs and to quantify their abundances provides invaluable information for understanding these signaling networks. Currently, mass spectrometry (MS) arguably serves as the most high-throughput and unbiased platform for studying PTMs. Here we detail experimental and analytical procedures for the characterization of lysine acetylation on proteins in general and on histones in particular, which are among the most highly modified proteins in eukaryotic cells.

Key words

Mass spectrometry Lysine acetylation Posttranslational modification Proteomics Histones