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Structure of the Centromere Binding Factor 3 Complex from Kluyveromyces lactis
Phong D Lee1, Hui Wei2, Dongyan Tan3
1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, 02115, USA; Graduate Program in Virology, Harvard Medical School, Boston, MA, 02115, USA.
Kinetochore protein complexes in budding yeast were structurally analyzed. Differences in the CBF3 complex between Kluyveromyces lactis and Saccharomyces cerevisiae were identified, explaining variations in centromere DNA.
Area of Science:
- Cell Biology
- Structural Biology
- Genetics
Background:
- Kinetochores are crucial multiprotein complexes linking centromeres to spindle microtubules during mitosis.
- Budding yeast centromeres contain three key elements: CDEI, CDEII, and CDEIII.
- Significant length variation exists in CDEII between Kluyveromyces lactis and Saccharomyces cerevisiae.
Purpose of the Study:
- To investigate the structural basis for differences in centromeric nucleosome assembly between K. lactis and S. cerevisiae.
- To understand how variations in centromere DNA elements influence kinetochore structure and function.
Main Methods:
- Determined the structure of the K. lactis CBF3 complex using electron cryomicroscopy (cryo-EM) at approximately 4 Å resolution.
- Compared the K. lactis CBF3 structure with published structures of the S. cerevisiae CBF3 complex.
Main Results:
- Identified distinct structural differences in the pose of the Ndc10 protein within the K. lactis CBF3 complex.
- Observed variations that may explain how the extended CDEII region in K. lactis centromeres is accommodated.
Conclusions:
- Structural insights into the K. lactis CBF3 complex reveal mechanisms for accommodating longer centromere DNA elements.
- These findings contribute to understanding the diversity of kinetochore assembly across different yeast species.
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