Journal
BIOPHYSICAL JOURNAL
Volume 88, Issue 3, Pages 2068-2077Publisher
CELL PRESS
DOI: 10.1529/biophysj.104.049759
Keywords
-
Categories
Ask authors/readers for more resources
Conventional kinesin has a double-headed structure consisting of two motor domains and moves processively along a microtubule using the two heads cooperatively. The movement of single and multiple truncated heads of Drosophila kinesin was measured using a laser trap and nanometer detecting apparatus. Single molecules of single-headed kinesin bound to the microtubules with a 3.5 nm biased displacement toward the plus end of the microtubule. The position of these single-headed kinesin molecules bound to a microtubule did not change until they had dissociated, indicating that single kinesin heads utilize nonprocessive movement processes. Two molecules of single-headed kinesin moved continuously along a microtubule with a lower velocity and force than that of single molecules of double-headed kinesin. The biased binding of the heads determines the directionality of movement, whereas two molecules of single-headed kinesin move continuously without dissociation from a microtubule.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available