CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere

Author:

Falk Samantha J.12,Guo Lucie Y.13,Sekulic Nikolina1,Smoak Evan M.134,Mani Tomoyasu13,Logsdon Glennis A.13,Gupta Kushol1,Jansen Lars E. T.5,Van Duyne Gregory D.13,Vinogradov Sergei A.13,Lampson Michael A.234,Black Ben E.123

Affiliation:

1. Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

2. Graduate Program in Cell and Molecular Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

3. Graduate Program in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

4. Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.

5. Instituto Gulbenkian de Ciência, 2780-156 Oeiras, Portugal.

Abstract

Building stable centromeres Each of our chromosomes has a single centromere, seen as a constriction during cell division, which is required for accurate chromosome segregation to daughter cells. Falk et al. show that the special histone protein known as CENP-A, which forms part of the nucleosomes at centromeres, makes the chromatin at these constrictions very stable and long-lived. This stability is conferred by a protein-binding partner, CENP-C, recruited to the centromere by the CENP-A histone. Binding of CENP-C to CENP-A–containing nucleosomes alters the behavior of the macromolecular centromere complex to help it maintain its identity Science , this issue p. 699

Funder

NSF

NIH

American Cancer Society

American Heart Association

European Research Council

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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