Revealing histone variant induced changes via quantitative proteomics

Anna M. Arnaudo, Rosalynn C. Molden, Benjamin A. Garcia

Research output: Contribution to journalReview articlepeer-review

25 Scopus citations

Abstract

Histone variants are isoforms of linker and core histone proteins that differ in their amino acid sequences. These variants have distinct genomic locations and posttranslational modifications, thus increasing the complexity of the chromatin architecture. Biological studies of histone variants indicate that they play a role in many processes including transcription, DNA damage response, and the cell cycle. The small differences in amino acid sequence and the diverse posttranslational modification states that exist between histone variants make traditional analysis using immunoassay methods challenging. In recent years, a number of mass spectrometric techniques have been developed to identify and quantify histones at the whole protein or peptide levels. In this review, we discuss the biology of histone variants and methods to characterize them using mass spectrometry-based proteomics.

Original languageEnglish
Pages (from-to)284-294
Number of pages11
JournalCritical Reviews in Biochemistry and Molecular Biology
Volume46
Issue number4
DOIs
StatePublished - Aug 2011

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