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Ndc10 is a platform for inner kinetochore assembly in budding yeast.

http://www.ncbi.nlm.nih.gov/pubmed/22139014

Kinetochores link centromeric DNA to spindle microtubules and ensure faithful chromosome segregation during mitosis. In point-centromere yeasts, the CBF3 complex Skp1-Ctf13-(Cep3)(2)-(Ndc10)(2) recognizes a conserved centromeric DNA element through contacts made by Cep3 and Ndc10. We describe here the five-domain organization of Kluyveromyces lactis Ndc10 and the structure at 2.8 Å resolution of domains I-II (residues 1-402) bound to DNA. The structure resembles tyrosine DNA recombinases, although it lacks both endonuclease and ligase activities. Structural and biochemical data demonstrate that each subunit of the Ndc10 dimer binds a separate fragment of DNA, suggesting that Ndc10 stabilizes a DNA loop at the centromere. We describe in vitro association experiments showing that specific domains of Ndc10 interact with each of the known inner-kinetochore proteins or protein complexes in budding yeast. We propose that Ndc10 provides a central platform for inner-kinetochore assembly.

Pubmed ID: 22139014 RIS Download

Mesh terms: Amino Acid Sequence | Binding Sites | Crystallography, X-Ray | DNA, Fungal | DNA-Binding Proteins | Electrophoresis, Polyacrylamide Gel | Electrophoretic Mobility Shift Assay | Fungal Proteins | Kinetochores | Kluyveromyces | Models, Molecular | Molecular Sequence Data | Mutation | Protein Binding | Protein Multimerization | Protein Structure, Tertiary | Sequence Homology, Amino Acid

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Associated grants

  • Agency: Howard Hughes Medical Institute, Id:
  • Agency: Howard Hughes Medical Institute, Id:

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