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• W4323534016 abstract "The enrichment of histone H3 variant CENP-A is the epigenetic mark of centromere and initiates the assembly of the kinetochore at centromere. The kinetochore is a multi-subunit complex that ensures accurate attachment of microtubule centromere and faithful segregation of sister chromatids during mitosis. As a subunit of kinetochore, CENP-I localization at centromere also depends on CENP-A. However, whether and how CENP-I regulates CENP-A deposition and centromere identity remains unclear. Here, we identified that CENP-I directly interacts with the centromeric DNA and preferentially recognizes AT-rich elements of DNA via a consecutive DNA-binding surface formed by conserved charged residues at the end of N-terminal HEAT repeats. The DNA binding–deficient mutants of CENP-I retained the interaction with CENP-H/K and CENP-M, but significantly diminished the centromeric localization of CENP-I and chromosome alignment in mitosis. Moreover, the DNA binding of CENP-I is required for the centromeric loading of newly synthesized CENP-A. CENP-I stabilizes CENP-A nucleosomes upon binding to nucleosomal DNA instead of histones. These findings unveiled the molecular mechanism of how CENP-I promotes and stabilizes CENP-A deposition and would be insightful for understanding the dynamic interplay of centromere and kinetochore during cell cycle." @default.
• W4323534016 created "2023-03-09" @default.
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• W4323534016 date "2023-03-08" @default.
• W4323534016 modified "2023-09-23" @default.
• W4323534016 title "CENP-I directly targets centromeric DNA to support CENP-A deposition and centromere maintenance" @default.
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• W4323534016 doi "https://doi.org/10.1073/pnas.2219170120" @default.
• W4323534016 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36888657" @default.
• W4323534016 hasPublicationYear "2023" @default.
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