The kinetochore module Okp1<sup>CENP-Q</sup>/Ame1<sup>CENP-U</sup> is a reader for N-terminal modifications on the centromeric histone Cse4<sup>CENP-A</sup>.
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ABSTRACT: Kinetochores are supramolecular assemblies that link centromeres to microtubules for sister chromatid segregation in mitosis. For this, the inner kinetochore CCAN/Ctf19 complex binds to centromeric chromatin containing the histone variant CENP-A, but whether the interaction of kinetochore components to centromeric nucleosomes is regulated by posttranslational modifications is unknown. Here, we investigated how methylation of arginine 37 (R37Me) and acetylation of lysine 49 (K49Ac) on the CENP-A homolog Cse4 from Saccharomyces cerevisiae regulate molecular interactions at the inner kinetochore. Importantly, we found that the Cse4 N-terminus binds with high affinity to the Ctf19 complex subassembly Okp1/Ame1 (CENP-Q/CENP-U in higher eukaryotes), and that this interaction is inhibited
SUBMITTER: Anedchenko EA
PROVIDER: S-EPMC6315295 | biostudies-literature | 2019 Jan
REPOSITORIES: biostudies-literature
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