Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Cell Biochem. 2004 Jul 1;92(4):691-700.

Application of mass spectrometry to the identification and quantification of histone post-translational modifications.

Author information

  • 1Department of Chemistry, The Ohio State University, Columbus, Ohio 43210, USA.

Abstract

The core histones are the primary protein component of chromatin, which is responsible for the packaging of eukaryotic DNA. The NH(2)-terminal tail domains of the core histones are the sites of numerous post-translational modifications that have been shown to play an important role in the regulation of chromatin structure. In this study, we discuss the recent application of modern analytical techniques to the study of histone modifications. Through the use of mass spectrometry, a large number of new sites of histone modification have been identified, many of which reside outside of the NH(2)-terminal tail domains. In addition, techniques have been developed that allow mass spectrometry to be effective for the quantitation of histone post-translational modifications. Hence, the use of mass spectrometry promises to dramatically alter our view of histone post-translational modifications.

Copyright 2004 Wiley-Liss, Inc.

PMID:
15211567
[PubMed - indexed for MEDLINE]
PMCID:
PMC2572815
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for John Wiley & Sons, Inc. Icon for PubMed Central
    Loading ...
    Write to the Help Desk