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Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3

Author

Listed:
  • Zheng Zhou

    (Laboratory of Biochemistry and Molecular Biology, National Cancer Institute)

  • Hanqiao Feng

    (Laboratory of Biochemistry and Molecular Biology, National Cancer Institute)

  • Bing-Rui Zhou

    (Laboratory of Biochemistry and Molecular Biology, National Cancer Institute)

  • Rodolfo Ghirlando

    (Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases)

  • Kaifeng Hu

    (National Magnetic Resonance Facility at Madison, University of Wisconsin)

  • Adam Zwolak

    (Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, NIH, Bethesda, Maryland 20892, USA)

  • Lisa M. Miller Jenkins

    (Laboratory of Cell Biology, National Cancer Institute, NIH, Bethesda, Maryland 20892, USA)

  • Hua Xiao

    (Laboratory of Biochemistry and Molecular Biology, National Cancer Institute)

  • Nico Tjandra

    (Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, NIH, Bethesda, Maryland 20892, USA)

  • Carl Wu

    (Laboratory of Biochemistry and Molecular Biology, National Cancer Institute)

  • Yawen Bai

    (Laboratory of Biochemistry and Molecular Biology, National Cancer Institute)

Abstract

Histone recognition on the centromere Centromeres, regions on the chromosome that are essential for accurate chromosome segregation, contain unique chromatin that is marked by a histone H3 variant termed CenH3 or CENP-A. The simple centromeres of budding yeast provide an attractive system for investigating centromere biology, including the pathway of CenH3 deposition and the architecture of the centromeric nucleosome. The chaperone Scm3 is required in budding yeast for the deposition of CenH3 (called Cse4) at centromeres. Zhou et al. present the nuclear magnetic resonance structure of Cse4 and histone H4 complexed with Scm3, and outline the structural basis for the recognition of Cse4 by Scm3. They propose a model for Scm3 function as a chaperone that has implications for the assembly of centromeric nucleosomes.

Suggested Citation

  • Zheng Zhou & Hanqiao Feng & Bing-Rui Zhou & Rodolfo Ghirlando & Kaifeng Hu & Adam Zwolak & Lisa M. Miller Jenkins & Hua Xiao & Nico Tjandra & Carl Wu & Yawen Bai, 2011. "Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3," Nature, Nature, vol. 472(7342), pages 234-237, April.
    • Handle: RePEc:nat:nature:v:472:y:2011:i:7342:d:10.1038_nature09854
    DOI: 10.1038/nature09854
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