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Structural mechanisms of centromeric nucleosome recognition by the kinetochore protein CENP-N.


ABSTRACT: Accurate chromosome segregation requires the proper assembly of kinetochore proteins. A key step in this process is the recognition of the histone H3 variant CENP-A in the centromeric nucleosome by the kinetochore protein CENP-N. We report cryo-electron microscopy (cryo-EM), biophysical, biochemical, and cell biological studies of the interaction between the CENP-A nucleosome and CENP-N. We show that human CENP-N confers binding specificity through interactions with the L1 loop of CENP-A, stabilized by electrostatic interactions with the nucleosomal DNA. Mutational analyses demonstrate analogous interactions in Xenopus, which are further supported by residue-swapping experiments involving the L1 loop of CENP-A. Our results are consistent with the coevolution of CENP-N and CENP-A and establish the structural basis for recognition of the CENP-A nucleosome to enable kinetochore assembly and centromeric chromatin organization.

SUBMITTER: Chittori S 

PROVIDER: S-EPMC6292214 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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Structural mechanisms of centromeric nucleosome recognition by the kinetochore protein CENP-N.

Chittori Sagar S   Hong Jingjun J   Saunders Hayden H   Feng Hanqiao H   Ghirlando Rodolfo R   Kelly Alexander E AE   Bai Yawen Y   Subramaniam Sriram S  

Science (New York, N.Y.) 20171221 6373


Accurate chromosome segregation requires the proper assembly of kinetochore proteins. A key step in this process is the recognition of the histone H3 variant CENP-A in the centromeric nucleosome by the kinetochore protein CENP-N. We report cryo-electron microscopy (cryo-EM), biophysical, biochemical, and cell biological studies of the interaction between the CENP-A nucleosome and CENP-N. We show that human CENP-N confers binding specificity through interactions with the L1 loop of CENP-A, stabil  ...[more]

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