Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3
Zheng Zhou,
Hanqiao Feng,
Bing-Rui Zhou,
Rodolfo Ghirlando,
Kaifeng Hu,
Adam Zwolak,
Lisa M. Miller Jenkins,
Hua Xiao,
Nico Tjandra,
Carl Wu and
Yawen Bai ()
Additional contact information
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
Nature, 2011, vol. 472, issue 7342, 234-237
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.
Date: 2011
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DOI: 10.1038/nature09854
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