Breaking the histone code with quantitative mass spectrometry

Laura Mae P. Britton, Michelle Gonzales-Cope, Barry M. Zee, Benjamin A. Garcia

Research output: Contribution to journalReview articlepeer-review

99 Scopus citations


Histone post-translational modifications (PTMs) comprise one of the most intricate nuclear signaling networks that govern gene expression in a long-term and dynamic fashion. These PTMs are considered to be epigenetic or heritable from one cell generation to the next and help establish genomic expression patterns. While much of the analyses of histones have historically been performed using site-specific antibodies, these methods are replete with technical obstacles (i.e., cross-reactivity and epitope occlusion). Mass spectrometry-based proteomics has begun to play a significant role in the interrogation of histone PTMs, revealing many new aspects of these modifications that cannot be easily determined with standard biological approaches. Here, we review the accomplishments of mass spectrometry in the histone field, and outline the future roadblocks that must be overcome for mass spectrometry-based proteomics to become the method of choice for chromatin biologists.

Original languageEnglish
Pages (from-to)631-643
Number of pages13
JournalExpert Review of Proteomics
Issue number5
StatePublished - Oct 2011


  • chromatin
  • combinatorial
  • discovery
  • epigenetic
  • histone
  • mass spectrometry
  • post-translational modification
  • proteomics
  • quantification


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