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. Author manuscript; available in PMC: 2010 Apr 8.
Published in final edited form as: Cell. 2006 Jul 28;126(2):335–348. doi: 10.1016/j.cell.2006.05.046

Figure 2. Artificial Dimerization of Dynein Monomers Induces Processive Movement.

Figure 2

(A) TMR-labeled FRB-Dyn1331 kDa plus rapamycin did not move processively in the single-molecule TIRF assay. Kymographs were made by horizontally stacking line scans along the axonemal axis. Some stationary dynein molecules were seen (vertical lines), but most molecules bound transiently, and no moving molecules were observed (see diagonal lines in Figure 2B).

(B) Dimerization of TMR-labeled FRB-Dyn1331 kDa and FKBP12-Dyn1331 kDa by rapamycin produces processive runs in the single-molecule TIRF assay. Diagonal lines in the kymograph represent dynein molecules that are moving along the axoneme over time (see also Movie S3). A histogram of rapamycin-dimerized dynein run lengths shows a run length of 1.2 ± 0.1 μm (mean ± SE; n = 223, Figure S3).