Single-molecule analysis of dynein processivity and stepping behavior. Export

@article{Reck-Peterson_DyneinProcessivity_Cell_2006, abstract = {Cytoplasmic dynein, the 1.2 MDa motor driving minus-end-directed motility, has been reported to move processively along microtubules, but its mechanism of motility remains poorly understood. Here, using S. cerevisiae to produce recombinant dynein with a chemically controlled dimerization switch, we show by structural and single-molecule analysis that processivity requires two dynein motor domains but not dynein's tail domain or any associated subunits. Dynein advances most frequently in 8 nm steps, although longer as well as side and backward steps are observed. Individual motor domains show a different stepping pattern, which is best explained by the two motor domains shuffling in an alternating manner between rear and forward positions. Our results suggest that cytoplasmic dynein moves processively through the coordination of its two motor domains, but its variable step size and direction suggest a considerable diffusional component to its step, which differs from Kinesin-1 and is more akin to myosin VI.}, address = {Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.}, author = {Reck-Peterson, S. L. and Yildiz, A. and Carter, A. P. and Gennerich, A. and Zhang, N. and Vale, R. D.}, citeulike-article-id = {2833475}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.cell.2006.05.046}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16873064}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16873064}, day = {28}, doi = {10.1016/j.cell.2006.05.046}, issn = {0092-8674}, journal = {Cell}, keywords = {behavior, dynein, processivity, stepping, vale}, month = {July}, number = {2}, pages = {335--348}, posted-at = {2008-05-26 11:39:39}, priority = {0}, title = {Single-molecule analysis of dynein processivity and stepping behavior.}, url = {http://dx.doi.org/10.1016/j.cell.2006.05.046}, volume = {126}, year = {2006} }

TY - JOUR ID - Reck-Peterson_DyneinProcessivity_Cell_2006 L3 - citeulike-article-id:2833475 N2 - Cytoplasmic dynein, the 1.2 MDa motor driving minus-end-directed motility, has been reported to move processively along microtubules, but its mechanism of motility remains poorly understood. Here, using S. cerevisiae to produce recombinant dynein with a chemically controlled dimerization switch, we show by structural and single-molecule analysis that processivity requires two dynein motor domains but not dynein's tail domain or any associated subunits. Dynein advances most frequently in 8 nm steps, although longer as well as side and backward steps are observed. Individual motor domains show a different stepping pattern, which is best explained by the two motor domains shuffling in an alternating manner between rear and forward positions. Our results suggest that cytoplasmic dynein moves processively through the coordination of its two motor domains, but its variable step size and direction suggest a considerable diffusional component to its step, which differs from Kinesin-1 and is more akin to myosin VI. IS - 2 JF - Cell SN - 0092-8674 AD - Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA. EP - 348 TI - Single-molecule analysis of dynein processivity and stepping behavior. VL - 126 SP - 335 KW - behavior KW - dynein KW - processivity KW - stepping KW - vale AU - Reck-Peterson, SL AU - Yildiz, A AU - Carter, AP AU - Gennerich, A AU - Zhang, N AU - Vale, RD PY - 2006/07/28/ UR - http://dx.doi.org/10.1016/j.cell.2006.05.046 ER -