Summary information and primary citation
- PDB-id
- 6buz; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- structural protein-DNA
- Method
- cryo-EM (3.92 Å)
- Summary
- cryo-EM structure of cenp-a nucleosome in complex with kinetochore protein cenp-n
- Reference
- Chittori S, Hong J, Saunders H, Feng H, Ghirlando R, Kelly AE, Bai Y, Subramaniam S (2018): "Structural mechanisms of centromeric nucleosome recognition by the kinetochore protein CENP-N." Science, 359, 339-343. doi: 10.1126/science.aar2781.
- 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.