Characterization of histones and their post-translational modifications by mass spectrometry

Benjamin A. Garcia, Jeffrey Shabanowitz, Donald F. Hunt

Research output: Contribution to journalReview articlepeer-review

118 Scopus citations

Abstract

Histone proteins and their accompanying post-translational modifications have received much attention for their ability to affect chromatin structure and, hence, regulate gene expression. Recently, mass spectrometry has become an important complementary tool for the analysis of histone variants and modification sites, for determining the degree of occupancy of these modifications and for quantifying differential expression of these modifications from various samples. Additionally, as advancements in mass spectrometry technologies continue, the ability to read entire 'histone codes' across large regions of histone polypeptides or intact protein is possible. As chromatin biology demands, mass spectrometry has adapted and continues as a key technology for the analysis of gene regulation networks involving histone modifications.

Original languageEnglish
Pages (from-to)66-73
Number of pages8
JournalCurrent Opinion in Chemical Biology
Volume11
Issue number1
DOIs
StatePublished - Feb 2007

Fingerprint

Dive into the research topics of 'Characterization of histones and their post-translational modifications by mass spectrometry'. Together they form a unique fingerprint.

Cite this