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CENP-B creates alternative epigenetic chromatin states permissive for CENP-A or heterochromatin assembly.

Authors
  • Otake, Koichiro1
  • Ohzeki, Jun-Ichirou1
  • Shono, Nobuaki1
  • Kugou, Kazuto1
  • Okazaki, Koei1
  • Nagase, Takahiro2
  • Yamakawa, Hisashi3
  • Kouprina, Natalay4
  • Larionov, Vladimir4
  • Kimura, Hiroshi5
  • Earnshaw, William C6
  • Masumoto, Hiroshi7
  • 1 Laboratory of Chromosome Engineering, Department of Frontier Research and Development, Kazusa DNA Research Institute, 2-6-7 Kazusa-Kamatari, Kisarazu 292-0818, Japan. , (Japan)
  • 2 Public Relations and Research Promotion Group, Kazusa DNA Research Institute, 2-6-7 Kazusa-Kamatari, Kisarazu 292-0818, Japan. , (Japan)
  • 3 Clinical Analysis Team, Department of Omics Research and Development, Kazusa DNA Research Institute, 2-6-7 Kazusa-Kamatari, Kisarazu 292-0818, Japan. , (Japan)
  • 4 Genome Structure and Function Group, Developmental Therapeutics Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
  • 5 Cell Biology Unit, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503, Japan. , (Japan)
  • 6 Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3BF, UK.
  • 7 Laboratory of Chromosome Engineering, Department of Frontier Research and Development, Kazusa DNA Research Institute, 2-6-7 Kazusa-Kamatari, Kisarazu 292-0818, Japan [email protected] , (Japan)
Type
Published Article
Journal
Journal of Cell Science
Publisher
The Company of Biologists
Publication Date
Aug 11, 2020
Volume
133
Issue
15
Identifiers
DOI: 10.1242/jcs.243303
PMID: 32661090
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

CENP-B binds to CENP-B boxes on centromeric satellite DNAs (known as alphoid DNA in humans). CENP-B maintains kinetochore function through interactions with CENP-A nucleosomes and CENP-C. CENP-B binding to transfected alphoid DNA can induce de novo CENP-A assembly, functional centromere and kinetochore formation, and subsequent human artificial chromosome (HAC) formation. Furthermore, CENP-B also facilitates H3K9 (histone H3 lysine 9) trimethylation on alphoid DNA, mediated by Suv39h1, at ectopic alphoid DNA integration sites. Excessive heterochromatin invasion into centromere chromatin suppresses CENP-A assembly. It is unclear how CENP-B controls such different chromatin states. Here, we show that the CENP-B acidic domain recruits histone chaperones and many chromatin modifiers, including the H3K36 methylase ASH1L, as well as the heterochromatin components Suv39h1 and HP1 (HP1α, β and γ, also known as CBX5, CBX1 and CBX3, respectively). ASH1L facilitates the formation of open chromatin competent for CENP-A assembly on alphoid DNA. These results indicate that CENP-B is a nexus for histone modifiers that alternatively promote or suppress CENP-A assembly by mutually exclusive mechanisms. Besides the DNA-binding domain, the CENP-B acidic domain also facilitates CENP-A assembly de novo on transfected alphoid DNA. CENP-B therefore balances CENP-A assembly and heterochromatin formation on satellite DNA. © 2020. Published by The Company of Biologists Ltd.

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