Epigenetic Regulation and Epigenomics
Published Online: 10 OCT 2011
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Reviews in Cell Biology and Molecular Medicine
How to Cite
Xhemalce, B., Dawson, M. A. and Bannister, A. J. 2011. Histone Modifications. Reviews in Cell Biology and Molecular Medicine. .
- Published Online: 10 OCT 2011
Histones are highly conserved small basic proteins that are found exclusively in eukaryotic cells, predominantly in the nucleus. First described in 1884 by Albrecht Kossel, using an avian red blood cell system, the histones help to overcome–at least in part–a fundamental problem experienced by the vast majority of eukaryotic cells–that is, how to package approximately 2 m of DNA within a relatively small nuclear volume. To achieve this, the DNA is complexed with histones and other proteins to form an ordered and compact structure termed chromatin. Chromatin serves to protect the DNA from damage, and also to regulate the access of factors that are important in the regulation of DNA processes, such as transcription, replication, and repair. It is now known that the histones–and especially their N-terminal “tails”–are subject to a plethora of post-translational modifications. In this chapter, these dynamic modifications are introduced together with the relevant enzymes, and the means by which they are integrated in order to elicit appropriate biological outcomes are discussed. In some cases, the modification directly perturbs chromatin structure, whereas in other cases it forms a dynamic binding platform that promotes, or indeed hinders, the recruitment of further histone-modifying enzymes. Finally, some of the severe consequences that can arise following the deregulation of the histone modification pathways are described.
- Chromatin immunoprecipitation (ChIP);
- Mass spectrometry (MS);
- Post-translational modification (PTM)