The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends.
In: Nature, Jg. 440 (2006-03-23), Heft 7083, S. 565-569
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Zugriff:
Chromosomes interact through their kinetochores with microtubule plus ends and they are segregated to the spindle poles as the kinetochore microtubules shorten during anaphase A of mitosis. The molecular natures and identities of coupling proteins that allow microtubule depolymerization to pull chromosomes to poles during anaphase have long remained elusive. In budding yeast, the ten-protein Dam1 complex is a critical microtubule-binding component of the kinetochore that oligomerizes into a 50-nm ring around a microtubule in vitro. Here we show, with the use of a real-time, two-colour fluorescence microscopy assay, that the ring complex moves processively for several micrometres at the ends of depolymerizing microtubules without detaching from the lattice. Electron microscopic analysis of ‘end-on views’ revealed a 16-fold symmetry of the kinetochore rings. This out-of-register arrangement with respect to the 13-fold microtubule symmetry is consistent with a sliding mechanism based on an electrostatically coupled ring–microtubule interface. The Dam1 ring complex is a molecular device that can translate the force generated by microtubule depolymerization into movement along the lattice to facilitate chromosome segregation. [ABSTRACT FROM AUTHOR]
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Titel: |
The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends.
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Autor/in / Beteiligte Person: | Westermann, Stefan ; Wang, Hong-Wei ; Avila-Sakar, Agustin ; Drubin, David G. ; Nogales, Eva ; Barnes, Georjana |
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Zeitschrift: | Nature, Jg. 440 (2006-03-23), Heft 7083, S. 565-569 |
Veröffentlichung: | 2006 |
Medientyp: | academicJournal |
ISSN: | 0028-0836 (print) |
DOI: | 10.1038/nature04409 |
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