How the kinetochore couples microtubule force and centromere stretch to move chromosomes
Autor: | Kerry Bloom, Aussie Suzuki, Tomoo Ohashi, Benjamin L. Badger, Harold P. Erickson, Julian Haase, Edward D. Salmon |
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Jazyk: | angličtina |
Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Centromere Cell Cycle Proteins Biology Microtubules Models Biological Time-Lapse Imaging Ndc80 complex Article 03 medical and health sciences 0302 clinical medicine Microtubule Fluorescence Resonance Energy Transfer Kinetochores Microtubule nucleation Binding Sites Kinetochore Nuclear Proteins Cell Biology Spindle apparatus Cell biology Microtubule plus-end NDC80 Kinetics Luminescent Proteins 030104 developmental biology Microscopy Fluorescence Mutation Saccharomycetales Chromosomes Fungal Microtubule-Associated Proteins 030217 neurology & neurosurgery Protein Binding |
Zdroj: | Nature cell biology |
ISSN: | 1476-4679 1465-7392 |
Popis: | The Ndc80 complex (Ndc80, Nuf2, Spc24 and Spc25) is a highly conserved kinetochore protein essential for end-on anchorage to spindle microtubule plus ends and for force generation coupled to plus-end polymerization and depolymerization. Spc24/Spc25 at one end of the Ndc80 complex binds the kinetochore. The N-terminal tail and CH domains of Ndc80 bind microtubules, and an internal domain binds microtubule-associated proteins (MAPs) such as the Dam1 complex. To determine how the microtubule- and MAP-binding domains of Ndc80 contribute to force production at the kinetochore in budding yeast, we have inserted a FRET tension sensor into the Ndc80 protein about halfway between its microtubule-binding and internal loop domains. The data support a mechanical model of force generation at metaphase where the position of the kinetochore relative to the microtubule plus end reflects the relative strengths of microtubule depolymerization, centromere stretch and microtubule-binding interactions with the Ndc80 and Dam1 complexes. |
Databáze: | OpenAIRE |
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