Microscopic analysis of binding mode of single kinesin molecules with microtubule
نویسندگان
چکیده
منابع مشابه
Thermal activation of single kinesin molecules with temperature pulse microscopy.
Conventional kinesin is a processive motor protein that keeps "walking" along a microtubule using chemical energy released by ATP hydrolysis. We previously studied the effects of temperature between 15 degrees and 35 degrees C on the moving velocity, force, and processivity of single kinesin molecules using a bead assay [Kawaguchi and Ishiwata, 2000b: Biochem Biophys Res Commun 272:895-899]. Ho...
متن کاملStructures of kinesin and kinesin-microtubule interactions.
Several X-ray crystal structures of kinesin motor domains have recently been solved at high resolution ( approximately 0.2-0.3 nm), in both their monomeric and dimeric states. They show the folding of the polypeptide chain and different arrangements of subunits in the dimer. In addition, cryo-electron microscopy and image reconstruction have revealed microtubules decorated with kinesin at inter...
متن کاملwoman-defined identity: analysis of selected poems of adrienne rich
the current thesis is composed in five chapters in the following fashion: chapter two encompasses the applied framework of the project in details; the methodology of carl gustav jung to explain the process of individuation, the major archetypes and their attributes and his techniques to assess the mind’s strata are all explained. moreover, the austrian psychoanalysts, heinz kohut’s models of a...
Identification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin.
The kinesin-binding site on the microtubule has not been identified because of the technical difficulties involved in the mutant analyses of tubulin. Exploiting the budding yeast expression system, we succeeded in replacing the negatively charged residues in the alpha-helix 12 of beta-tubulin with alanine and analyzed their effect on kinesin-microtubule interaction in vitro. The microtubule gli...
متن کاملKar3Vik1, a member of the Kinesin-14 superfamily, shows a novel kinesin microtubule binding pattern
Kinesin-14 motors generate microtubule minus-end-directed force used in mitosis and meiosis. These motors are dimeric and operate with a nonprocessive powerstroke mechanism, but the role of the second head in motility has been unclear. In Saccharomyces cerevisiae, the Kinesin-14 Kar3 forms a heterodimer with either Vik1 or Cik1. Vik1 contains a motor homology domain that retains microtubule bin...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2000
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.40.s68_3