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Post-Translational Modifications in Health and Disease pp 365–385Cite as

Regulation of Chromatin Structure and Transcription Via Histone Modifications

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Part of the book series: Protein Reviews ((PRON,volume 13))

Abstract

Chromatin, which was once considered merely a structural component required for DNA packaging, is now recognized as a dynamic template governed by intricate regulation. Histone post-translational modifications (PTMs) contribute to chromatin dynamics and regulate fundamental biological processes including transcription, mitotic chromatin condensation and DNA repair following damage. To date, histone methylation, acetylation, phosphorylation, ubiquitination, sumoylation and ADP-ribosylation, among others, have been described – and the list continues to grow. The last decade has witnessed an explosion in the discovery and characterization of histone PTMs, the enzymatic machinery and binding effectors responsible for their regulation, as well as unexpected mechanisms of histone regulation, such as lysine demethylation and histone tail clipping. This chapter focuses on the regulation of well-characterized histone PTMs, and their roles in the context of transcription and chromatin structure.

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Acknowledgements

The authors wish to thank Matthew Goldberg, Luis Duarte, Andrew Xiao and Sandra Hake for discussions and critical reading of this chapter. We apologize to those whose work could not be cited due to space limitations. This work was supported by The Ellison Medical Foundation and the American Skin Association to E.B.

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  1. Department of Oncological Sciences, Mount Sinai School of Medicine, New York, NY, 10029, USA

    Emily Bernstein

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  1. Kajan Ratnakumar
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  2. Avnish Kapoor
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  3. Emily Bernstein
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Correspondence to Emily Bernstein .

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  1. Depto. Quimica Inorganica, Universidad Murcia, Murcia, Spain

    Cecilio J. Vidal

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Ratnakumar, K., Kapoor, A., Bernstein, E. (2011). Regulation of Chromatin Structure and Transcription Via Histone Modifications. In: Vidal, C. (eds) Post-Translational Modifications in Health and Disease. Protein Reviews, vol 13. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-6382-6_15

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