title: To step or not to step? How biochemistry and mechanics influence processivity in Kinesin and Eg5.
abstract: Conventional kinesin and Eg5 are essential nanoscale motor proteins. Single-molecule and presteady-state kinetic experiments indicate that both motors use similar strategies to generate movement along microtubules, despite having distinctly different in vivo functions. Single molecules of kinesin, a long-distance cargo transporter, are highly processive, binding the microtubule and taking 100 or more sequential steps at velocities of up to 700 nm/s before dissociating, whereas Eg5, a motor active in mitotic spindle assembly, is also processive, but takes fewer steps at a slower rate. By dissecting the structural, biochemical and mechanical features of these proteins, we hope to learn how kinesin and Eg5 are optimized for their specific biological tasks, while gaining insight into how biochemical energy is converted into mechanical work.
authors.affiliation: Department of Biological Sciences Stanford University 030 Herrin Labs Stanford, CA 94305 650-724-5536 USA.
authors.forename: Megan T
authors.initials: MT
authors.lastname: Valentine
authors.forename: Susan P
authors.initials: SP
authors.lastname: Gilbert
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena; D019281:Dimerization; D016547:Kinesins / Q000502:physiology*; D008870:Microtubules / Q000502:physiology*; D011485:Protein Binding; D008941:Spindle Apparatus / Q000502:physiology
chemical_list: D016547:Kinesins