Single-Molecule Analysis of a Novel Kinesin Motor Protein Public Deposited

http://ir.library.oregonstate.edu/concern/undergraduate_thesis_or_projects/zk51vj215

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  • Kinesins are intracellular motor proteins that transform chemical energy into mechanical energy through ATP hydrolysis to move along microtubules. Kinesin roles can vary among transportation, regulation, and spindle alignment within most cells. Many kinesin have been found to move towards the plus end of microtubules at a steady velocity. For this experiment, we investigate BimC - a kinesin-5 associated with mitotic spindle regulation - under high salt conditions. Using single molecule imaging with Total Internal Reflection Fluorescence Microscopy, we found BimC to be directed towards the minus end of microtubules at a high velocity of 597 214 nm/s (mean S.D, n=124). BimC then joins the few other kinesin found so far to be minus-end-directed. However, preliminary results at low salt conditions suggest that BimC switches towards the plus end. BimC could very well be an early example of a kinesin motor protein that is directionally-dependent upon ionic strength. These results suggest multiple branches of further investigation into directionally-dependent kinesin proteins and what purposes they might have.
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