Force studies of multiple kinesin-1 and EG5 molecular motors
Graves, Evan Taclibon
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https://hdl.handle.net/2142/27741
Description
Title
Force studies of multiple kinesin-1 and EG5 molecular motors
Author(s)
Graves, Evan Taclibon
Issue Date
2009
Doctoral Committee Chair(s)
Ha, Taekjip
Committee Member(s)
Selvin, Paul R.
Oono, Yoshitsugu
Giannetta, Russell W.
Department of Study
Physics
Discipline
Physics
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
molecular motors
Language
en
Abstract
Kinesin-1 and Eg5 are molecular motors that are essential for eukaryotic cell growth and development. Kinesin-1 motors transport intracellular cargo along the microtubule cytoskeleton through and against the dense viscoelastic cytoplasm. Eg5 motors mediate proper mitotic, microtubule spindle assembly during cell division, and then stabilize these spindle structures through a balance between plus-end directed and minus-end directed forces along the filaments. Therefore, it is impmiant to understand how multiple kinesin-1 and Eg5 motors withstand competing forces, their structural rigidity under such loads, and how quickly they are able to rebind ifloosed from microtubules. Using a unique type of analysis for our optical trapping experiments, we are able to get motor binding stoichiometry inaccessible by previous techniques. With this information we characterize both motors comparing them to one another. We find that the release forces for both types of motors add linearly with the number of motors bound and that Eg5 has a weaker binding than that of kinesin -1. The stiffuess for the motor domains is comparable, yet we find that the average time to rebind for Eg5 decreases at higher concentrations while it does not for kinesin-1. This may indicate that there exists some weak interaction between kinesin-1 and microtubules keeping them close while unbound.
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