Recognition of centromere-specific histone Cse4 by the inner kinetochore Okp1-Ame1 complex.
Successful mitosis depends on the timely establishment of correct chromosomal attachments to microtubules. The kinetochore, a modular multiprotein complex, mediates this connection by recognizing specialized chromatin containing a histone H3 variant called Cse4 in budding yeast and CENP-A in vertebrates. Structural features of the kinetochore that enable discrimination between Cse4/CENP-A ... and H3 have been identified in several species. How and when these contribute to centromere recognition and how they relate to the overall structure of the inner kinetochore are unsettled questions. More generally, this molecular recognition ensures that only one kinetochore is built on each chromatid and that this happens at the right place on the chromatin fiber. We have determined the crystal structure of a Cse4 peptide bound to the essential inner kinetochore Okp1-Ame1 heterodimer from budding yeast. The structure and related experiments show in detail an essential point of Cse4 contact and provide information about the arrangement of the inner kinetochore.
Mesh Terms:
Cell Cycle Proteins, Centromere, Centromere Protein A, Chromatin, Chromosomal Proteins, Non-Histone, DNA-Binding Proteins, Histones, Kinetochores, Saccharomyces cerevisiae Proteins, Saccharomycetales
Cell Cycle Proteins, Centromere, Centromere Protein A, Chromatin, Chromosomal Proteins, Non-Histone, DNA-Binding Proteins, Histones, Kinetochores, Saccharomyces cerevisiae Proteins, Saccharomycetales
EMBO Rep
Date: Dec. 06, 2023
PubMed ID: 37983946
View in: Pubmed Google Scholar
Download Curated Data For This Publication
247123
Switch View:
- Interactions 9