6BUZ

Cryo-EM structure of CENP-A nucleosome in complex with kinetochore protein CENP-N

Summary for 6BUZ

• Entry DOI: 10.2210/pdb6buz/pdb
• EMDB information: 7293
• Descriptor: Histone H3-like centromeric protein A, Histone H4, Histone H2A, ... (7 entities in total)
• Functional Keywords: structural protein-dna complex, histone fold, centromeric nucleosome, kinetochore, structural protein/dna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 11
• Total formula weight: 281737.05

Authors

Chittori, S.,Hong, J.,Kelly, A.E.,Bai, Y.,Subramaniam, S. (deposition date: 2017-12-11, release date: 2017-12-20, Last modification date: 2024-03-13)

Primary citation

Chittori, S.,Hong, J.,Saunders, H.,Feng, H.,Ghirlando, R.,Kelly, A.E.,Bai, Y.,Subramaniam, S.
Structural mechanisms of centromeric nucleosome recognition by the kinetochore protein CENP-N.
Science, 359:339-343, 2018

PubMed 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 , 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.

PubMed: 29269420
DOI: 10.1126/science.aar2781

Experimental method

ELECTRON MICROSCOPY (3.92 Å)