Motor protein–dependent ribosome motility. (A) Co-motility of Rpl25-GFP (Rpl25; green in Merge) and Rps3-mCherry₃ (Rps3; red in Merge). Both subunits travel together in a bidirectional fashion. Brightness, contrast, and gamma settings were adjusted. The photobleached area is indicated by “Bleach” and the red arrows. See Video 1. (B) Motility of Rpl25-GFP in the presence of the MT inhibitor benomyl and the solvent DMSO (Control). Motility is abolished in the absence of MTs. Cells were prebleached to reduce the background (“Bleach”). Images are contrast-inverted, and brightness, contrast, and gamma settings were adjusted. (C) Motility of Rpl25-GFP–labeled ribosomes in hyphal cells grown at 28°C (Control) and 32°C/2 h (Control, 32°C) in kinesin-3–null mutants (ΔKin3), and in temperature-sensitive dynein mutants at 32°C/2 h (Dyn2^ts, 32°C). Images are contrast-inverted, and brightness, contrast, and gamma settings were adjusted. (D) Flux rates of Rpl25-GFP in control cells, kinesin-3–null mutants (ΔKin3), and temperature-sensitive dynein mutants (Dyn2^ts) after 2 h a at restrictive temperature (32°C). Note that the bars show the combined flux in anterograde and retrograde direction. All bars are given as mean ± SEM (error bars) from a single representative experiment. Sample size is indicated. ***, significant difference to control at P < 0.0001 using a Student’s t test.