Journal
NUCLEIC ACIDS RESEARCH
Volume 43, Issue 10, Pages 4909-4922Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkv405
Keywords
-
Categories
Funding
- MEXT KAKENHI [25116002, 23247030, 23114008]
- MEXT, Japan
- Waseda Research Institute for Science and Engineering
- Uehara Foundation
- Naito Foundation
- Japan Society for the Promotion of Science [25-3931]
- Kazusa DNA Research Institute Foundation
- Intramural Research Program of the NIH, NCI, CCR
- Grants-in-Aid for Scientific Research [13J03931, 23247030, 26840025] Funding Source: KAKEN
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available