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      Effects of Surface Passivation on Gliding Motility Assays

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      Author(s): * , ,
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      Publication date (Electronic):
      Journal: PLoS ONE
      Publisher: Public Library of Science

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          Abstract

          In this study, we report differences in the observed gliding speed of microtubules dependent on the choice of bovine casein used as a surface passivator. We observed differences in both speed and support of microtubules in each of the assays. Whole casein, comprised of α s1, α s2, β, and κ casein, supported motility and averaged speeds of 966±7 nm/s. Alpha casein can be purchased as a combination of α s1 and α s2 and supported gliding motility and average speeds of 949±4 nm/s. Beta casein did not support motility very well and averaged speeds of 870±30 nm/s. Kappa casein supported motility very poorly and we were unable to obtain an average speed. Finally, we observed that mixing alpha, beta, and kappa casein with the proportions found in bovine whole casein supported motility and averaged speeds of 966±6 nm/s.

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          Kinesin walks hand-over-hand.

          Ahmet Yildiz, Michio Tomishige, Ronald D. Vale … (2004)
          Kinesin is a processive motor that takes 8.3-nm center-of-mass steps along microtubules for each adenosine triphosphate hydrolyzed. Whether kinesin moves by a "hand-over-hand" or an "inchworm" model has been controversial. We have labeled a single head of the kinesin dimer with a Cy3 fluorophore and localized the position of the dye to within 2 nm before and after a step. We observed that single kinesin heads take steps of 17.3 +/- 3.3 nm. A kinetic analysis of the dwell times between steps shows that the 17-nm steps alternate with 0-nm steps. These results strongly support a hand-over-hand mechanism, and not an inchworm mechanism. In addition, our results suggest that kinesin is bound by both heads to the microtubule while it waits for adenosine triphosphate in between steps.
          Article 0 comments Cited 193 times – based on 0 reviews     Review now
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            Mechanics of the kinesin step.

            N. J. Carter, R. A. Cross (2005)
            Kinesin is a molecular walking machine that organizes cells by hauling packets of components directionally along microtubules. The physical mechanism that impels directional stepping is uncertain. We show here that, under very high backward loads, the intrinsic directional bias in kinesin stepping can be reversed such that the motor walks sustainedly backwards in a previously undescribed mode of ATP-dependent backward processivity. We find that both forward and backward 8-nm steps occur on the microsecond timescale and that both occur without mechanical substeps on this timescale. The data suggest an underlying mechanism in which, once ATP has bound to the microtubule-attached head, the other head undergoes a diffusional search for its next site, the outcome of which can be biased by an applied load.
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              Kinesin moves by an asymmetric hand-over-hand mechanism.

              S Fehr, Whitney M Block, Charles Asbury (2003)
              Kinesin is a double-headed motor protein that moves along microtubules in 8-nanometer steps. Two broad classes of model have been invoked to explain kinesin movement: hand-over-hand and inchworm. In hand-over-hand models, the heads exchange leading and trailing roles with every step, whereas no such exchange is postulated for inchworm models, where one head always leads. By measuring the stepwise motion of individual enzymes, we find that some kinesin molecules exhibit a marked alternation in the dwell times between sequential steps, causing these motors to "limp" along the microtubule. Limping implies that kinesin molecules strictly alternate between two different conformations as they step, indicative of an asymmetric, hand-over-hand mechanism.
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                Author and article information

                Contributors
                : Role: Editor
                Journal
                Journal ID (nlm-ta): PLoS One
                Journal ID (publisher-id): plos
                Journal ID (pmc): plosone
                Title: PLoS ONE
                Publisher: Public Library of Science (San Francisco, USA )
                ISSN (Electronic): 1932-6203
                Publication date Collection: 2011
                Publication date (Electronic): 3 June 2011
                Volume: 6
                Issue: 6
                Electronic Location Identifier: e19522
                Affiliations
                [1]Department of Physics and Astronomy and Center for High Technology Materials, University of New Mexico, Albuquerque, New Mexico, United States of America
                Dalhousie University, Canada
                Author notes

                Conceived and designed the experiments: AM SJK. Performed the experiments: AM. Analyzed the data: AM LJH SJK. Contributed reagents/materials/analysis tools: AM LJH SJK. Wrote the paper: AM LJH SJK. Designed the software used in the analysis: LJH SJK.

                Article
                Publisher ID: PONE-D-10-05135
                DOI: 10.1371/journal.pone.0019522
                PMC ID: 3108588
                PubMed ID: 21674032
                SO-VID: f2578ec0-4e6c-4267-ac19-a7d4b3d16634
                Copyright © Maloney et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
                History
                Date received : 18 November 2010
                Date accepted : 6 April 2011
                Page count
                Pages: 8
                Categories
                Subject: Research Article
                Subject: Biology
                Subject: Biochemistry
                Subject: Metabolism
                Subject: Biological Transport
                Subject: Biophysics
                Subject: Cell Motility
                Subject: Microtubules
                Subject: Neuroscience
                Subject: Motor Systems
                Subject: Chemistry
                Subject: Physical Chemistry
                Subject: Chemical Properties
                Subject: Intermolecular Forces
                Subject: Materials Science
                Subject: Biomaterials
                Subject: Glass Science
                Subject: Physics
                Subject: Biophysics
                Subject: Cell Motility
                Subject: Microtubules
                Subject: Macromolecular Assemblies

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