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The Dam1 ring binds microtubules strongly enough to be a processive as well as energy-efficient coupler for chromosome motionстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
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Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 3 декабря 2015 г.
- Авторы: Grishchuk E.L., Efremov A.K., Volkov V.A., Spiridonov I.S., Gudimchuk N., Westermann S., Drubin D., Barnes G., McIntosh J.R., Ataullakhanov F.I.
- Журнал: Proceedings of the National Academy of Sciences of the United States of America
- Том: 105
- Номер: 40
- Год издания: 2008
- Издательство: National Academy of Sciences
- Местоположение издательства: United States
- Первая страница: 15423
- Последняя страница: 15428
- DOI: 10.1073/pnas.0807859105
- Аннотация: Accurate chromosome segregation during mitotic division of budding yeast depends on the multiprotein kinetochore complex, Dam1 (also known as DASH). Purified Dam1 heterodecamers encircle microtubules (MTs) to form rings that can function as "couplers," molecular devices that transduce energy from MT disassembly into the motion of a cargo. Here we show that MT depolymerization develops a force against a Dam1 ring that is sixfold larger than the force exerted on a coupler that binds only one side of an MT. Wild-type rings slow depolymerization fourfold, but rings that include a mutant Dam1p with truncated C terminus slow depolymerization less, consistent with the idea that this tail is part of a strong bond between rings and MTs. A molecular-mechanical model for Dam1-MT interaction predicts that binding between this flexible tail and the MT wall should cause a Dam1 ring to wobble, and Fourier analysis of moving, ring-attached beads corroborates this prediction. Comparison of the forces generated against wild-type and mutant complexes confirms the importance of tight Dam1-MT association for processive cargo movement under load
- Добавил в систему: Атауллаханов Фазоил Иноятович