Stable complex formation of CENP-B with the CENP-A nucleosome

CENP-A and CENP-B are major components of centromeric chromatin. CENP-A is the histone H3 variant, which forms the centromere-specific nucleosome. CENP-B specifically binds to the CENP-B box DNA sequence on the centromere-specific repetitive DNA. In the present study, we found that the CENP-A nucleo...

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Bibliographic Details
Published in:Nucleic acids research 2015-05, Vol.43 (10), p.4909-4922
Main Authors: Fujita, Risa, Otake, Koichiro, Arimura, Yasuhiro, Horikoshi, Naoki, Miya, Yuta, Shiga, Tatsuya, Osakabe, Akihisa, Tachiwana, Hiroaki, Ohzeki, Jun-ichirou, Larionov, Vladimir, Masumoto, Hiroshi, Kurumizaka, Hitoshi
Format: Article
Language:English
Subjects:
Autoantigens - chemistry
Autoantigens - metabolism
Cell Line, Tumor
Centromere - chemistry
Centromere Protein A
Centromere Protein B - metabolism
Chromosomal Proteins, Non-Histone - chemistry
Chromosomal Proteins, Non-Histone - metabolism
DNA - chemistry
DNA - metabolism
Gene regulation, Chromatin and Epigenetics
Histones - metabolism
Humans
Nucleosomes - metabolism
Protein Interaction Domains and Motifs
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Summary:CENP-A and CENP-B are major components of centromeric chromatin. CENP-A is the histone H3 variant, which forms the centromere-specific nucleosome. CENP-B specifically binds to the CENP-B box DNA sequence on the centromere-specific repetitive DNA. In the present study, we found that the CENP-A nucleosome more stably retains human CENP-B than the H3.1 nucleosome in vitro. Specifically, CENP-B forms a stable complex with the CENP-A nucleosome, when the CENP-B box sequence is located at the proximal edge of the nucleosome. Surprisingly, the CENP-B binding was weaker when the CENP-B box sequence was located in the distal linker region of the nucleosome. This difference in CENP-B binding, depending on the CENP-B box location, was not observed with the H3.1 nucleosome. Consistently, we found that the DNA-binding domain of CENP-B specifically interacted with the CENP-A-H4 complex, but not with the H3.1-H4 complex, in vitro. These results suggested that CENP-B forms a more stable complex with the CENP-A nucleosome through specific interactions with CENP-A, if the CENP-B box is located proximal to the CENP-A nucleosome. Our in vivo assay also revealed that CENP-B binding in the vicinity of the CENP-A nucleosome substantially stabilizes the CENP-A nucleosome on alphoid DNA in human cells.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkv405