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TitleStructural mechanisms of centromeric nucleosome recognition by the kinetochore protein CENP-N.
Journal, issue, pagesScience, Vol. 359, Issue 6373, Page 339-343, Year 2018
Publish dateJan 19, 2018
AuthorsSagar Chittori / Jingjun Hong / Hayden Saunders / Hanqiao Feng / Rodolfo Ghirlando / Alexander E Kelly / Yawen Bai / Sriram Subramaniam /
PubMed AbstractAccurate 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 ...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 , 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.
External linksScience / PubMed:29269420 / PubMed Central
MethodsEM (single particle)
Resolution3.92 Å
Structure data

7293

6buz

EMDB-7293, PDB-6buz:
Cryo-EM structure of CENP-A nucleosome in complex with kinetochore protein CENP-N
Method: EM (single particle) / Resolution: 3.92 Å

Source
  • homo sapiens (human)
  • synthetic construct (others)
  • escherichia coli (E. coli)
KeywordsSTRUCTURAL PROTEIN/DNA / STRUCTURAL PROTEIN-DNA complex / Histone fold / Centromeric nucleosome / Kinetochore

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