Highly processive motility is not a general feature of the kinesins
dc.contributor.author | Stewart, Russell J. | en_US |
dc.contributor.author | Schmidt, Christoph F. | en_US |
dc.date.accessioned | 2006-09-08T19:55:44Z | |
dc.date.available | 2006-09-08T19:55:44Z | |
dc.date.issued | 1998-06 | en_US |
dc.identifier.citation | Stewart, R. J.; Schmidt, Christoph F.; (1998). "Highly processive motility is not a general feature of the kinesins." European Biophysics Journal 27(4): 353-360. <http://hdl.handle.net/2027.42/42061> | en_US |
dc.identifier.issn | 0175-7571 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/42061 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9691464&dopt=citation | en_US |
dc.description.abstract | Evidence is presented that the kinesin-related ncd protein is not as processive as kinesin. In low surface density motility experiments, a dimeric ncd fusion protein behaved mechanistically more similar to non-processive myosins than to the highly processive kinesin. First, there was a critical microtubule length for motility; only microtubules longer than this critical length moved in low density ncd surfaces, which suggested that multiple ncd proteins must cooperate to move microtubules in the surface assay. Under similar conditions, native kinesin demonstrated no critical microtubule length, consistent with the behavior of a highly processive motor. Second, addition of methylcellulose to decrease microtubule diffusion decreased the critical microtubule length for motility. Also, the rates of microtubule motility were microtubule length dependent in methylcellulose; short microtubules, that interacted with fewer ncd proteins, moved more slowly than long microtubules that interacted with more ncd proteins. In contrast, short microtubules, that interacted with one or a few kinesin proteins, moved on average slightly faster than long microtubules that interacted with multiple kinesins. We conclude that a degree of processivity as high as that of kinesin, where a single dimer can move over distances on the order of one micrometer, may not be a general mechanistic feature of the kinesin superfamily. | en_US |
dc.format.extent | 188770 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Springer-Verlag; Springer-Verlag Berlin Heidelberg | en_US |
dc.subject.other | Microtubules | en_US |
dc.subject.other | Legacy | en_US |
dc.subject.other | Key Words Ncd Protein | en_US |
dc.subject.other | Kinesins | en_US |
dc.subject.other | In Vitro Motility | en_US |
dc.subject.other | Processivity | en_US |
dc.title | Highly processive motility is not a general feature of the kinesins | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Genetics | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Biophysical Research Division, University of Michigan, Ann Arbor, MI 48109, USA e-mail: cfs@umich.edu, US | en_US |
dc.contributor.affiliationother | Department of Bioengineering, University of Utah, Salt Lake City, UT 84112, USA e-mail: rstewart@ee.utah.edu, US | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 9691464 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/42061/1/249-27-4-353_80270353.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/s002490050142 | en_US |
dc.identifier.source | European Biophysics Journal | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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