Linked Life Data

11823639

Source:http://linkedlifedata.com/resource/pubmed/id/11823639

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5556
pubmed:dateCreated
2002-2-1
pubmed:abstractText
The motor enzyme kinesin makes hundreds of unidirectional 8-nanometer steps without detaching from or freely sliding along the microtubule on which it moves. We investigated the kinesin stepping mechanism by immobilizing a Drosophila kinesin derivative through the carboxyl-terminal end of the neck coiled-coil domain and measuring orientations of microtubules moved by single enzyme molecules at submicromolar adenosine triphosphate concentrations. The kinesin-mediated microtubule-surface linkage was sufficiently torsionally stiff (>/=2.0 +/- 0.9 x 10(-20) Newton meters per radian2) that stepping by the hypothesized symmetric hand-over-hand mechanism would produce 180 degree rotations of the microtubule relative to the immobilized kinesin neck. In fact, there were no rotations, a finding that is inconsistent with symmetric hand-over-hand movement. An alternative "inchworm" mechanism is consistent with our experimental results.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
295
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
844-8
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Distinguishing inchworm and hand-over-hand processive kinesin movement by neck rotation measurements.
pubmed:affiliation
Biophysics and Structural Biology Program, Biochemistry Department, Brandeis University, Waltham, MA 02454-9110, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.