Figure 1: Motile properties of heterodimeric dynein constructs bearing a single ATPase mutation.
From: Tension on the linker gates the ATP-dependent release of dynein from microtubules
(a) Dynein monomers truncated at the N-terminal tail are dimerized through an N-terminal GST tag (orange). The nucleotide-gating model requires the ATPase cycles of the two heads to be kept out of phase. (b) A schematic (right) of FRB-FKBP12 dynein heterodimer on a MT. One of the heads (blue) contains specific mutations at an ATPase site. (c) Average velocity (±s.e.m.) and run length (±95% CI) of TMR-labelled dynein motors at 2 mM ATP. One WT monomer is dimerized with a partner carrying the indicated ATPase mutation. (d) Kymographs showing the processive movement of WT/WT and AAA1K/A/WT motors. (e) Plot of velocity versus run termination rate for the indicated heterodimers shows a linear relationship (black line).
