Supplementary information : A torque component in the kinesin-1 power stroke : Nature Chemical Biology

From the following article

A torque component in the kinesin-1 power stroke

Junichiro Yajima & Robert A Cross

Nature Chemical Biology 1, 338 - 341 (2005) Published online: 9 October 2005

doi:10.1038/nchembio740

Supplementary Fig. 1

RK340-Sp1 binding to DNA (a) Gel mobility shift assay of RK340-Sp1 binding to an 80 bp double stranded DNA that included the Sp1 GC box recognition sequence (0, 1, 5, 10, 20, 40, 70, and 100 nM proteins in lane 0-7, respectively). (b) Apparent equilibrium binding curve obtained by calculating the fraction of DNA bound at varying RK340-Sp1 concentrations. The binding constant was determined by fitting to the equation Ø_b = [protein] / ([protein] + K_d) to obtain the dissociation constant (Kd). The observed dissociation constant was K_d = 21 plusminus 6 nM, which was close to the value as reported previously [Richard W. et al. (1992) PNAS 89 9759-63].

Supplementary Fig. 1 - Download PDF file (44KB)

Supplementary Video 1

Microtubule rotation driven by RK340Gel. The scale bar is 2 m. The time code is hours : minutes : seconds : centiseconds.

Supplementary Video 1 - Download Movie (4MB)

Supplementary Video 2

Sliding of a microtubule blocked in rotation. The arrow moving south-north marks a microtubule with a long side-arm that is unable to rotate. Sliding continues (see text) at close to wild type velocity. The arrow moving west-east tracks a microtubule with a short side-arm that is rotating normally. Time code and scale bar as in Supplementary Video 1.

Supplementary Video 2 - Download Movie (3MB)