Letter | Published:

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

Nature volume 383, pages 269272 (19 September 1996) | Download Citation

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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 information

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

    • Diane G. Edmondson
    •  & Sharon Y. Roth

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https://doi.org/10.1038/383269a0

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