BIOPHYSICS AND COMPUTATIONAL BIOLOGY Correction for “Measuring collective transport by defined numbers of processive and nonprocessive kinesin motors,” by Ken’ya Furuta, Akane Furuta, Yoko Y. Toyoshima, Misako Amino, Kazuhiro Oiwa, and Hiroaki Kojima which appeared in issue 2, January 8, 2013, of Proc Natl Acad Sci USA (110:501–506; first published December 24, 2012; 10.1073/pnas.1201390110).
The authors note that Fig. 3 appeared incorrectly. The graph legends for 1 kinesin and 2 kinesins in Fig. 3D were swapped. The corrected figure and its legend appear below.
Fig. 3.
Optical trapping assays. (A) Schematic of the typical experimental setup for optical trapping assays (not drawn to scale). (B) Time traces of optical trapping assays for (from top to bottom) one, two, three, or four kinesin-1 dimer(s) linked by rigid DNA scaffolds (∼6-nm spacing). Traces were acquired at 10 kHz (gray) and median-filtered to 25 Hz (black). The positive value corresponds to the force toward the MT plus-end (bead diameter, 0.45 μm; trap stiffness, 0.05–0.182 pN⋅nm−1). (C) Time traces of optical trapping assays for Ncd linked by rigid DNA scaffolds (∼6-nm spacing). Arrowheads show examples of binding events (bead diameter, 0.21 μm; trap stiffness, 0.014–0.027 pN⋅nm−1). (D) Histogram of the average maximum force generated by kinesin-1. The motors are linked by rigid DNA scaffolds (∼6-nm spacing). The numbers in the legend represent the number of motors in the assemblies. Inset: Average maximum forces (mean ± SEM) are plotted vs. motor number. Black and red colors represent intermotor spacings of 6.1–7.0 nm and 22.1–22.7 nm, respectively (SI Appendix, Fig. S4). The spacing between motors did not appear to affect the on-rate unlike in the low load condition, probably because of the difference in the arrangement of the motors on the trapped bead. (E) Histogram of the average maximum force generated by Ncd. The motors are linked by rigid DNA scaffolds (∼6-nm spacing). The color scheme and symbol are the same as in D. N.D., not determined.