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- W2966793669 abstract "Summary Centromeres are microtubule attachment sites on chromosomes defined by the enrichment of CENP-A-containing nucleosomes. To preserve centromere identity, CENP-A must be escorted to centromeres by a CENP-A-specific chaperone for deposition. Despite this essential requirement, many eukaryotes differ in the composition of players involved in centromere maintenance highlighting the plasticity of this process. In humans, CENP-A recognition and centromere targeting is achieved by HJURP and the Mis18 complex, respectively. Here, using crystal structures, we show how Drosophila CAL1, an evolutionarily distinct CENP-A chaperone, targets CENP-A to the centromere receptor CENP-C without the requirement of the Mis18 complex: while the N-terminal CAL1 fragment (CAL1 1-160 ) wraps around CENP-A/H4 through multiple physical contacts, the C-terminal CAL1 fragment (CAL1 893-914 ) directly binds CENP-C cupin dimer. Our work shows CAL1, though divergent at the primary structure, employs evolutionarily conserved and adaptive structural principles to recognise CENP-A/H4 and CENP-C providing insights into the minimalistic principles underlying centromere maintenance." @default.
- W2966793669 created "2019-08-13" @default.
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- W2966793669 date "2019-08-02" @default.
- W2966793669 modified "2023-10-06" @default.
- W2966793669 title "Structural Basis for CAL1-Mediated Centromere Maintenance" @default.
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- W2966793669 doi "https://doi.org/10.1101/723213" @default.
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