Journal
NATURE COMMUNICATIONS
Volume 10, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-09824-4
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Funding
- Darwin Trust of Edinburgh
- Darwin Trust
- European Commission Network of Excellence EpiGeneSys [HEALTH-F4-2010-257082]
- Wellcome Enhancement Award [095021]
- Wellcome [203149]
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/N016858/1]
- Wellcome Investigator Award [110064/Z/15/Z]
- Cancer Center Support Grant [5P30CA045508]
- Principal's Career Development scholarship
- Wellcome Trust [110064/Z/15/Z] Funding Source: Wellcome Trust
- BBSRC [BB/N016858/1] Funding Source: UKRI
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Despite the conserved essential function of centromeres, centromeric DNA itself is not conserved. The histone-H3 variant, CENP-A, is the epigenetic mark that specifies centromere identity. Paradoxically, CENP-A normally assembles on particular sequences at specific genomic locations. To gain insight into the specification of complex centromeres, here we take an evolutionary approach, fully assembling genomes and centromeres of related fission yeasts. Centromere domain organization, but not sequence, is conserved between Schizosaccharomyces pombe, S. octosporus and S. cryophilus with a central CENP-A(Cnp1) domain flanked by heterochromatic outer-repeat regions. Conserved syntenic clusters of tRNA genes and 5S rRNA genes occur across the centromeres of S. octosporus and S. cryophilus, suggesting conserved function. Interestingly, nonhomologous centromere central-core sequences from S. octosporus and S. cryophilus are recognized in S. pombe, resulting in cross-species establishment of CENP-A(Cnp1) chromatin and functional kinetochores. Therefore, despite the lack of sequence conservation, Schizosaccharomyces centromere DNA possesses intrinsic conserved properties that promote assembly of CENP-A chromatin.
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