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Histone acetylation in chromatin structure and transcription

Nature volume 389, pages 349–352 (1997)Cite this article

Abstract

The amino termini of histones extend from the nucleosomal core and are modified by acetyltransferases and deacetylases during the cell cycle. These acetylation patterns may direct histone assembly and help regulate the unfolding and activity of genes.

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Figure 1: Recognition of the acetylated H3/H4 complex by human CAF1.
Figure 2: Preferential acetylation of H4 K12 in heterochromatin.
Figure 3: Transcription factors and repression by histone H3/H4 deacetylation.

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Acknowledgements

I thank A. Berk, J. Kadonaga, G. Felsenfeld, S. Rundlett and A. Carmen for comments.

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  1. the Department of Biological Chemistry, UCLA School of Medicine and the Molecular Biology Institute, University of California, Los Angeles, 90095, California, USA

    Michael Grunstein

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Grunstein, M. Histone acetylation in chromatin structure and transcription. Nature 389, 349–352 (1997). https://doi.org/10.1038/38664

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