Structure of the Centromere Binding Factor 3 Complex from Kluyveromyces lactis |
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| Institution: | 1. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, 02115, USA;2. Graduate Program in Virology, Harvard Medical School, Boston, MA, 02115, USA;3. The National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, 10027, USA;4. Department of Pharmacological Sciences, Stony Brook University School of Medicine, Stony Brook, NY, 11794, USA;5. Howard Hughes Medical Institute, Harvard Medical School, Boston, MA, 02115, USA;1. State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, PR China;2. Guangdong Provincial Key Laboratory of Marine Biology, Shantou University, Shantou, PR China;3. Marine Biology Institute, Shantou University, Shantou, PR China;4. Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, Xiamen, PR China;5. South China Sea Bio-Resource Exploitation and Utilization Collaborative Innovation Center, Xiamen, PR China;6. State Key Laboratory of Ocean Engineering, School of Naval Architecture, Ocean and Civil Engineering, Shanghai Jiao Tong University, Shanghai, PR China |
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| Abstract: | Kinetochores are the multiprotein complexes that link chromosomal centromeres to mitotic-spindle microtubules. Budding yeast centromeres comprise three sequential "centromere-determining elements", CDEI, II, and III. CDEI (8 bp) and CDEIII (∼ 25 bp) are conserved between Kluyveromyces lactis and Saccharomyces cerevisiae, but CDEII in the former is twice as long (160 bp) as CDEII in the latter (80 bp). The CBF3 complex recognizes CDEIII and is required for assembly of a centromeric nucleosome, which in turn recruits other kinetochore components. To understand differences in centromeric nucleosome assembly between K. lactis and S. cerevisiae, we determined the structure of a K. lactis CBF3 complex by electron cryomicroscopy at ∼ 4 Å resolution and compared it with published structures of S. cerevisiae CBF3. We show differences in the pose of Ndc10 and discuss potential models of the K. lactis centromeric nucleosome that account for the extended CDEII length. |
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