Disorder in CENP-ACse4 tail-chaperone interaction facilitates binding with Ame1/Okp1 at the kinetochore.
The centromere is epigenetically marked by a histone H3 variant-CENP-A. The budding yeast CENP-A called Cse4, consists of an unusually long N-terminus that is known to be involved in kinetochore assembly. Its disordered chaperone, Scm3 is responsible for the centromeric deposition of Cse4 as well as in the maintenance of ... a segregation-competent kinetochore. In this study, we show that the Cse4 N-terminus is intrinsically disordered and interacts with Scm3 at multiple sites, and the complex does not gain any substantial structure. Additionally, the complex forms a synergistic association with an essential inner kinetochore component (Ctf19-Mcm21-Okp1-Ame1), and a model has been suggested to this effect. Thus, our study provides mechanistic insights into the Cse4 N-terminus-chaperone interaction and also illustrates how intrinsically disordered proteins mediate assembly of complex multiprotein networks, in general.
Mesh Terms:
Binding Sites, Cell Cycle Proteins, Centromere Protein A, Chromosomal Proteins, Non-Histone, Cytoskeletal Proteins, DNA-Binding Proteins, Intrinsically Disordered Proteins, Kinetochores, Microtubule-Associated Proteins, Models, Molecular, Molecular Chaperones, Protein Binding, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Binding Sites, Cell Cycle Proteins, Centromere Protein A, Chromosomal Proteins, Non-Histone, Cytoskeletal Proteins, DNA-Binding Proteins, Intrinsically Disordered Proteins, Kinetochores, Microtubule-Associated Proteins, Models, Molecular, Molecular Chaperones, Protein Binding, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Structure
Date: Jun. 06, 2024
PubMed ID: 38565139
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