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Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation

Author

Listed:
  • Marilyn G. Pray-Grant

    (University of Virginia School of Medicine)

  • Jeremy A. Daniel

    (University of Virginia School of Medicine)

  • David Schieltz

    (Diversa Corporation)

  • John R. Yates

    (The Scripps Research Institute)

  • Patrick A. Grant

    (University of Virginia School of Medicine)

Abstract

The specific post-translational modifications to histones influence many nuclear processes including gene regulation, DNA repair and replication1. Recent studies have identified effector proteins that recognize patterns of histone modification and transduce their function in downstream processes2. For example, histone acetyltransferases (HATs) have been shown to participate in many essential cellular processes, particularly those associated with activation of transcription3. Yeast SAGA (Spt-Ada-Gcn5 acetyltransferase) and SLIK (SAGA-like) are two highly homologous and conserved multi-subunit HAT complexes, which preferentially acetylate histones H3 and H2B and deubiquitinate histone H2B. Here we identify the chromatin remodelling protein Chd1 (chromo-ATPase/helicase-DNA binding domain 1) as a component of SAGA and SLIK. Our findings indicate that one of the two chromodomains of Chd1 specifically interacts with the methylated lysine 4 mark on histone H3 that is associated with transcriptional activity. Furthermore, the SLIK complex shows enhanced acetylation of a methylated substrate and this activity is dependent upon a functional methyl-binding chromodomain, both in vitro and in vivo. Our study identifies the first chromodomain that recognizes methylated histone H3 (Lys 4) and possibly identifies a larger subfamily of chromodomain proteins with similar recognition properties.

Suggested Citation

  • Marilyn G. Pray-Grant & Jeremy A. Daniel & David Schieltz & John R. Yates & Patrick A. Grant, 2005. "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation," Nature, Nature, vol. 433(7024), pages 434-438, January.
    • Handle: RePEc:nat:nature:v:433:y:2005:i:7024:d:10.1038_nature03242
    DOI: 10.1038/nature03242
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    Cited by:

    1. Corina Maritz & Reihaneh Khaleghi & Michelle N. Yancoskie & Sarah Diethelm & Sonja Brülisauer & Natalia Santos Ferreira & Yang Jiang & Shana J. Sturla & Hanspeter Naegeli, 2023. "ASH1L-MRG15 methyltransferase deposits H3K4me3 and FACT for damage verification in nucleotide excision repair," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Shijia Zhu & Guohua Wang & Bo Liu & Yadong Wang, 2013. "Modeling Exon Expression Using Histone Modifications," PLOS ONE, Public Library of Science, vol. 8(6), pages 1-15, June.

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