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The structure of the yeast Ctf3 complex.

Stephen M Hinshaw1, Andrew N Dates2, Stephen C Harrison1

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Howard Hughes Medical Institute, Boston, United States.

Elife
|June 14, 2019
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Summary
This summary is machine-generated.

Researchers detailed the Ctf3 complex structure, revealing molecular insights into how inner kinetochore proteins assemble and function at chromosomal attachment sites for spindle microtubules.

Keywords:
Cryo-EMKinetochoreMitosisS. cerevisiaemolecular biophysicsstructural biology

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • Kinetochores serve as crucial microtubule attachment sites and regulate cell cycle transitions.
  • Kinetochore function relies on conserved protein factors, divided into inner and outer complexes.
  • Inner kinetochore proteins identify assembly sites via specialized nucleosomes (Cse4/CENP-A).

Purpose of the Study:

  • To determine the near-atomic structure of the yeast Ctf3 complex, an outer component of the Ctf19 complex (CCAN).
  • To provide a molecular understanding of Ctf3 complex recruitment and its role in kinetochore assembly and function.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to resolve the structure of the Ctf3 complex.
  • High-resolution structural data enabled detailed molecular interpretation.

Main Results:

  • A near-atomic model of the Ctf3 complex was generated.
  • The model provides insights into the structural organization of the outermost Ctf19c sub-assembly.
  • The determined structure facilitates understanding of Ctf3's role in kinetochore function.

Conclusions:

  • The near-atomic structure of the Ctf3 complex offers a detailed view of inner kinetochore architecture.
  • This structural information is key to interpreting the molecular mechanisms of Ctf3 recruitment and function at the kinetochore.