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Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

Nature volume 383, pages 269–272 (1996)Cite this article

Abstract

THE yeast transcriptional adaptor1–3, Gcn5p, is a catalytic subunit of a nuclear (type A) histone acetyltransferase linking histone acetylation to gene activation4–6. Here we report that Gcn5p acetylates histones H3 and H4 non-randomly at specific lysines in the amino-terminal domains. Lysine 14 of H3 and lysines 8 and 16 of H4 are highly preferred acetylation sites for Gcn5p. We also demonstrate that lysine 9 is the preferred position of acetylation in newly synthesized yeast H3 in vivo. This finding, along with the fact that lysines 5 and 12 in H4 are predominant acetylation sites during chromatin assembly of many organisms7–11, indicates that Gcn5p acetylates a distinct set of lysines that do not overlap with those sites characteristically used by type B histone acetyltransferase s for histone deposition and chromatin assembly.

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Author notes

  1. Diane G. Edmondson & Sharon Y. Roth

    Present address: Zoology Department, University of British Columbia, 6270 University Boulevard, Vancouver, BC, V6T1Z4, Canada

Authors and Affiliations

  1. Department of Biology, University of Rochester, Rochester, New York, 14627, USA

    Min-Hao Kuo, James E. Brownell, Richard E. Sobel, Tamara A. Ranalli & C. David Allis

  2. Department of Microbiology and Immunology, Baylor College of Medicine, Houston, Texas, 77030, USA

    Richard E. Sobel

  3. Department of Biochemistry and Molecular Biology, M. D. Anderson Cancer Center, Houston, Texas, 77030, USA

    Richard G. Cook

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Kuo, MH., Brownell, J., Sobel, R. et al. Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines. Nature 383, 269–272 (1996). https://doi.org/10.1038/383269a0

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