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Jun 27, 2015;4 e06845.

H2A histone-fold and DNA elements in nucleosome activate SWR1-mediated H2A.Z replacement in budding yeast.

Anand Ranjan, Feng Wang, Gaku Mizuguchi, Debbie Wei, Yingzi Huang, Carl Wu
Author Information
  1. Anand Ranjan: Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.
  2. Feng Wang: Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, United States.
  3. Gaku Mizuguchi: Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.
  4. Debbie Wei: Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, United States.
  5. Yingzi Huang: Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, United States.
  6. Carl Wu: Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.
PMID: 26116819 DOI: 10.7554/eLife.06845

Abstract

The histone variant H2A.Z is a universal mark of gene promoters, enhancers, and regulatory elements in eukaryotic chromatin. The chromatin remodeler SWR1 mediates site-specific incorporation of H2A.Z by a multi-step histone replacement reaction, evicting histone H2A-H2B from the canonical nucleosome and depositing the H2A.Z-H2B dimer. Binding of both substrates, the canonical nucleosome and the H2A.Z-H2B dimer, is essential for activation of SWR1. We found that SWR1 primarily recognizes key residues within the α2 helix in the histone-fold of nucleosomal histone H2A, a region not previously known to influence remodeler activity. Moreover, SWR1 interacts preferentially with nucleosomal DNA at superhelix location 2 on the nucleosome face distal to its linker-binding site. Our findings provide new molecular insights on recognition of the canonical nucleosome by a chromatin remodeler and have implications for ATP-driven mechanisms of histone eviction and deposition.

Keywords

H2A.Z S. cerevisiae biochemistry chromatin remodeler chromosomes genes nucleosome

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Grants

  1. /Howard Hughes Medical Institute
  2. /Intramural NIH HHS

MeSH Term

Adenosine Triphosphatases
Chromatin
Chromatin Assembly and Disassembly
DNA
Histones
Nucleosomes
Protein Binding
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins

Chemicals

Chromatin
Histones
Nucleosomes
Saccharomyces cerevisiae Proteins
DNA
Adenosine Triphosphatases
Swr1 protein, S cerevisiae
Journal Article Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't
Article has an altmetric score of 1

Word Cloud

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