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Structure of the Centromere Binding Factor 3 Complex from Kluyveromyces lactis
Ist Teil von
Journal of molecular biology, 2019-11, Vol.431 (22), p.4444-4454
Ort / Verlag
Netherlands: Elsevier Ltd
Erscheinungsjahr
2019
Quelle
MEDLINE
Beschreibungen/Notizen
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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•CBF3 complex required for centromeric nucleosome assembly in point-centromere yeast.•Cryo-EM structure of the Kluyveromyces lactis CBF3 complex.•CBF3 may induce substantial bend in DNA when mediating nucleosome assembly.