A Conserved Mechanism for Centromeric Nucleosome Recognition by Centromere Protein CENP-C

Author:

Kato Hidenori1,Jiang Jiansheng2,Zhou Bing-Rui1,Rozendaal Marieke3,Feng Hanqiao1,Ghirlando Rodolfo4,Xiao T. Sam2,Straight Aaron F.3,Bai Yawen1

Affiliation:

1. Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, Bethesda, MD 20892, USA.

2. Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892, USA.

3. Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.

4. Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.

Abstract

Kinetochore Targeting Chromosomes must be segregated accurately during cell division. This is facilitated by the attachment of mitotic spindle microtubules to the kinetochore at the chromosomal centromere. The centromere is marked with the histone H3 variant CenH3 (CENP-A in human), and CENP-C forms part of the inner kinetochore. Kato et al. (p. 1110 ) used structural biology, biochemistry, and mutagenesis to show that CENP-C recognizes CENP-A chromatin via several different interactions. The CENP-C "central domain" makes close contact with the acidic patch of histones H2A/H2B, and the highly conserved "CENP-C motif" senses both the acidic patch and recognizes the hydrophobicity of the otherwise nonconserved CenH3 tail, supporting a conserved mechanism of centromere targeting by the kinetochore.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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