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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.
Original language | English |
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Pages (from-to) | 2869-2880 |
Number of pages | 12 |
Journal | Nucleic Acids Research |
Volume | 41 |
Issue number | 5 |
DOIs | |
Publication status | Published - 2013 |
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Dive into the research topics of 'Nap1 regulates proper CENP-B binding to nucleosomes'. Together they form a unique fingerprint.Projects
- 5 Finished
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Core funding renewal for the Wellcome Trust Centre for Cell Biology
1/10/11 → 30/04/17
Project: Research
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The role of non-histone proteins in chromosome structure and function during mitosis
1/01/11 → 30/09/16
Project: Research