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Coupling of ATP hydrolysis to microt...
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Hunter, Andrew William.
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Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin./
作者:
Hunter, Andrew William.
面頁冊數:
109 p.
附註:
Chair: Linda Wordeman.
Contained By:
Dissertation Abstracts International63-08B.
標題:
Biology, Cell. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3062952
ISBN:
0493814892
Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin.
Hunter, Andrew William.
Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin.
- 109 p.
Chair: Linda Wordeman.
Thesis (Ph.D.)--University of Washington, 2002.
MCAK belongs to the Kin I subfamily of kinesin-related proteins, a unique group of motor proteins that are not motile but instead induce microtubule depolymerization. In the presence of ATP, MCAK binds to both ends of microtubules and has one high affinity site (<italic>K</italic><sub>d</sub> = 1 nM) per protofilament end. MCAK targets microtubule ends very quickly (<italic>k</italic><sub>on</sub> = 7.8 × 10<super>8</super> M<super> −1</super> s<super>−1</super>) by diffusion along the microtubule lattice. Once at a protofilament end MCAK acts as a processive depolymerase, removing tens of tubulin dimers, at a maximum rate of 1 s<super>−1</super> per MCAK dimer, before dissociating. MCAK has a low basal ATPase activity which is stimulated 10-fold by free tubulin and 350-fold by microtubule ends. Coupling of MCAK depolymerase activity to ATP hydrolysis revealed that five ATPs are required to remove each tubulin dimer from microtubules that resemble the GTP-cap thought to stabilize microtubules during growth. Our results show how the kinesin crossbridge cycle has been adapted to target MCAK to microtubule ends and utilize ATP hydrolysis to power microtubule depolymerization rather than directed motility.
ISBN: 0493814892Subjects--Topical Terms:
1017686
Biology, Cell.
Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin.
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MCAK belongs to the Kin I subfamily of kinesin-related proteins, a unique group of motor proteins that are not motile but instead induce microtubule depolymerization. In the presence of ATP, MCAK binds to both ends of microtubules and has one high affinity site (<italic>K</italic><sub>d</sub> = 1 nM) per protofilament end. MCAK targets microtubule ends very quickly (<italic>k</italic><sub>on</sub> = 7.8 × 10<super>8</super> M<super> −1</super> s<super>−1</super>) by diffusion along the microtubule lattice. Once at a protofilament end MCAK acts as a processive depolymerase, removing tens of tubulin dimers, at a maximum rate of 1 s<super>−1</super> per MCAK dimer, before dissociating. MCAK has a low basal ATPase activity which is stimulated 10-fold by free tubulin and 350-fold by microtubule ends. Coupling of MCAK depolymerase activity to ATP hydrolysis revealed that five ATPs are required to remove each tubulin dimer from microtubules that resemble the GTP-cap thought to stabilize microtubules during growth. Our results show how the kinesin crossbridge cycle has been adapted to target MCAK to microtubule ends and utilize ATP hydrolysis to power microtubule depolymerization rather than directed motility.
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