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Nap1 regulates proper CENP-B binding to nucleosomes

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  • Hiroaki Tachiwana
  • Yuta Miya
  • Nobuaki Shono
  • Jun-Ichirou Ohzeki
  • Akihisa Osakabe
  • Koichiro Otake
  • Vladimir Larionov
  • William C Earnshaw
  • Hiroshi Kimura
  • Hiroshi Masumoto
  • Hitoshi Kurumizaka

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Original languageEnglish
Pages (from-to)2869-2880
Number of pages12
JournalNucleic Acids Research
Volume41
Issue number5
DOIs
Publication statusPublished - 2013

Abstract

CENP-B is a widely conserved centromeric satellite DNA-binding protein, which specifically binds to a 17-bp DNA sequence known as the CENP-B box. CENP-B functions positively in the de novo assembly of centromeric nucleosomes, containing the centromere-specific histone H3 variant, CENP-A. At the same time, CENP-B also prevents undesired assembly of the CENP-A nucleosome through heterochromatin formation on satellite DNA integrated into ectopic sites. Therefore, improper CENP-B binding to chromosomes could be harmful. However, no CENP-B eviction mechanism has yet been reported. In the present study, we found that human Nap1, an acidic histone chaperone, inhibited the non-specific binding of CENP-B to nucleosomes and apparently stimulated CENP-B binding to its cognate CENP-B box DNA in nucleosomes. In human cells, the CENP-B eviction activity of Nap1 was confirmed in model experiments, in which the CENP-B binding to a human artificial chromosome or an ectopic chromosome locus bearing CENP-B boxes was significantly decreased when Nap1 was tethered near the CENP-B box sequence. In contrast, another acidic histone chaperone, sNASP, did not promote CENP-B eviction in vitro and in vivo and did not stimulate specific CENP-B binding to CENP-A nucleosomes in vitro. We therefore propose a novel mechanism of CENP-B regulation by Nap1.

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