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The mammalian centromere: structural domains and the attenuation of chromatin modeling

AARON A. VAN HOOSER^*, MICHAEL A. MANCINI^*, C. DAVID ALLIS, KEVIN F. SULLIVAN and B. R. BRINKLEY¹

^* Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA;
Department of Medicine, Biochemistry, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908, USA;
Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA

¹Correspondence: Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA. E-mail: brinkley{at}bcm.tmc.edu

The centromere-kinetochore complex can be divided into distinct domains based on structure and function. Previous work has used CREST auto-antibodies with various microscopic techniques to map the locations of proteins within the centromere-kinetochore complex and to analyze the maturation of prekinetochores before mitosis. Here we have focused on the centromere-specific histone Centromere Protein (CENP)-A and its spatial relationship to other histones and histone modifications found in condensed chromatin. We demonstrate that the phosphorylation of histone H3 is essentially excluded from a specific region of centromeric chromatin, defined by the presence of CENP-A. Interspersion of CENP-B with phosphorylated H3 in the inner centromere indicates that the exclusion of H3 modification is not a general property of -satellite DNA. We also demonstrate that these regions are functionally distinct by fragmenting mitotic chromatin into motile centromere-kinetochore fragments that contain CENP-A with little or no phosphorylated H3 and nonmotile fragments that contain exclusively phosphorylated H3. The sequence of CENP-A diverges from H3 in a number of key residues involved in chromosome condensation and in transcription, potentially allowing a more specialized chromatin structure within centromeric heterochromatin, on which kinetochore plates may nucleate and mature. This specialized centromere subdomain would be predicted to have a very tight and static nucleosome structure as a result of the absence of H3 phosphorylation and acetylation.—Van Hooser, A. A., Mancini, M. A., Allis, C. D., Sullivan, K. F., Brinkley, B. R. The mammalian centromere: structural domains and the attenuation of chromatin modeling.

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