Journal
NUCLEIC ACIDS RESEARCH
Volume 42, Issue 3, Pages 1644-1655Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkt1124
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Funding
- Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan
- Cabinet Office, Government of Japan
- International Human Frontier Science Program Organization
- MEXT
- PRESTO of JST
- MEXT, Japan
- Grants-in-Aid for Scientific Research [25280109, 11J06154, 24651151, 25116002, 13J05186] Funding Source: KAKEN
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The centromere is a specific genomic region upon which the kinetochore is formed to attach to spindle microtubules for faithful chromosome segregation. To distinguish this chromosomal region from other genomic loci, the centromere contains a specific chromatin structure including specialized nucleosomes containing the histone H3 variant CENP-A. In addition to CENP-A nucleosomes, we have found that centromeres contain a nucleosome-like structure comprised of the histone-fold CENP-T-W-S-X complex. However, it is unclear how the CENPT-W-S-X complex associates with centromere chromatin. Here, we demonstrate that the CENPT-W-S-X complex binds preferentially to similar to 100 bp of linker DNA rather than nucleosome-bound DNA. In addition, we find that the CENP-T-W-S-X complex primarily binds to DNA as a (CENP-T-W-S-X) 2 structure. Interestingly, in contrast to canonical nucleosomes that negatively supercoil DNA, the CENP-T-W-S-X complex induces positive DNA supercoils. We found that the DNA-binding regions in CENP-T or CENP-W, but not CENP-S or CENP-X, are required for this positive supercoiling activity and the kinetochore targeting of the CENP-T-W-S-X complex. In summary, our work reveals the structural features and properties of the CENP-T-W-S-X complex for its localization to centromeres.
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