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The language of covalent histone modifications

Nature volume 403, pages 41–45 (2000)Cite this article

Abstract

Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of these highly conserved modifications has remained elusive, converging biochemical and genetic evidence suggests functions in several chromatin-based processes. We propose that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events.

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Figure 1: Chromatin organization and the tail of histone H3.
Figure 2: The ‘histone code’ hypothesis.
Figure 3: Coordinated recruitment of histone-modifying activities.

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Acknowledgements

Research surrounding this topic in our laboratory is supported by grants from the NIH to C.D.A. and B.D.S. We wish to thank current laboratory members, especially C. A. Mizzen, for critical review of this manuscript, and T. K. Archer and C. L. Smith for kindly sharing unpublished data.

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  1. Department of Biochemistry and Molecular Genetics, University of Virginia Health Science Center, Charlottesville, 22908, Virginia, USA

    Brian D. Strahl & C. David Allis

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Correspondence to C. David Allis.

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Strahl, B., Allis, C. The language of covalent histone modifications. Nature 403, 41–45 (2000). https://doi.org/10.1038/47412

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