Dynamic instability of sheared microtubules observed by quasi-elastic light scattering.
The kinetics of microtubule reassembly was studied in vitro by quasi-elastic light scattering (QELS). When microtubules assembled in the absence of microtubule-associated proteins (MAPs) were sheared, they rapidly depolymerized, recovered, and reassembled. The mean length of the recovered microtubules was the same as that observed just before shearing, implying that on average one fragment per original microtubule survived the fragmentation and recovery. When microtubules that contained 25 percent brain MAP were sheared, the fragments did not depolymerize extensively and the average length of the fragments decreased by a factor of 3 relative to the unsheared sample. The results support the dynamic instability model, which predicts that cellular microtubules are latently unstable structures protected on their ends by stabilizing caps.
Department of Chemistry and Biochemistry, University of Guelph, Ontario, Canada.
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RA
Keates
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Hallett
D000818:Animals; D006153:Guanosine Diphosphate / Q000502:physiology; D006160:Guanosine Triphosphate / Q000502:physiology; D066298:In Vitro Techniques; D007700:Kinetics; D008027:Light; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism*; D012542:Scattering, Radiation; D014404:Tubulin / Q000378:metabolism
D008869:Microtubule-Associated Proteins; D014404:Tubulin; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate