The Saccharomyces cerevisiae histone H2A variant Htz1 is acetylated by NuA4

S. cerevisiae
  1. Michael-Christopher Keogh1,
  2. Thomas A. Mennella1,
  3. Chika Sawa1,7,
  4. Sharon Berthelet2,
  5. Nevan J. Krogan3,
  6. Adam Wolek4,
  7. Vladimir Podolny1,
  8. Laura Rocco Carpenter4,
  9. Jack F. Greenblatt5,6,
  10. Kristin Baetz2, and
  11. Stephen Buratowski1,8
  1. 1 Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA;
  2. 2 Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada;
  3. 3 Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco 94143, California, USA;
  4. 4 Upstate USA Inc., Lake Placid, New York 12946, USA;
  5. 5 Banting and Best Department of Medical Research
  6. 6 Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario M5G 1L6, Canada

    Abstract

    The histone H2A variant H2A.Z (Saccharomyces cerevisiae Htz1) plays roles in transcription, DNA repair, chromosome stability, and limiting telomeric silencing. The Swr1-Complex (SWR-C) inserts Htz1 into chromatin and shares several subunits with the NuA4 histone acetyltransferase. Furthermore, mutants of these two complexes share several phenotypes, suggesting they may work together. Here we show that NuA4 acetylates Htz1 Lys 14 (K14) after the histone is assembled into chromatin by the SWR-C. K14 mutants exhibit specific defects in chromosome transmission without affecting transcription, telomeric silencing, or DNA repair. Function-specific modifications may help explain how the same component of chromatin can function in diverse pathways.

    Keywords

    Footnotes

    • 7

      ↵7 Present address: Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.

    • 8

      ↵8 Corresponding author.

      ↵8 E-MAIL steveb{at}hms.harvard.edu; FAX (617) 738-0516.

    • Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1388106

      • Received October 26, 2005.
      • Accepted January 20, 2006.
    | Table of Contents

    This Article

    1. doi: 10.1101/gad.1388106 Genes & Dev. 20: 660-665 Copyright © 2006, Cold Spring Harbor Laboratory Press

    Article Category

    Share

    Current Issue

    1. March 1, 2024, 38 (5-6)
    1. Current Issue
    1. Alert me to new issues of G&D

    Life Science Alliance