RESUMO
Gliding motility in Myxococcus xanthus is powered by flagella stator homologs that move in helical trajectories using proton motive force. The Frz chemosensory pathway regulates the cell polarity axis through MglA, a Ras family GTPase; however, little is known about how MglA establishes the polarity of gliding, because the gliding motors move simultaneously in opposite directions. Here we examined the localization and dynamics of MglA and gliding motors in high spatial and time resolution. We determined that MglA localizes not only at the cell poles, but also along the cell bodies, forming a decreasing concentration gradient toward the lagging cell pole. MglA directly interacts with the motor protein AglR, and the spatial distribution of AglR reversals is positively correlated with the MglA gradient. Thus, the motors moving toward lagging cell poles are less likely to reverse, generating stronger forward propulsion. MglB, the GTPase-activating protein of MglA, regulates motor reversal by maintaining the MglA gradient. Our results suggest a mechanism whereby bacteria use Ras family proteins to modulate cellular polarity.
Assuntos
Proteínas de Bactérias/fisiologia , Proteínas Motores Moleculares/fisiologia , Myxococcus xanthus/fisiologia , Proteínas de Bactérias/genética , Corpo Celular/fisiologia , Polaridade Celular/fisiologia , Microscopia de Fluorescência , Modelos Biológicos , Proteínas Motores Moleculares/genética , Movimento/fisiologia , Myxococcus xanthus/citologia , Myxococcus xanthus/genética , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Proteínas ras/genética , Proteínas ras/fisiologiaRESUMO
Many bacterial species use gliding motility in natural habitats because external flagella function poorly on hard surfaces. However, the mechanism(s) of gliding remain elusive because surface motility structures are not apparent. Here, we characterized the dynamics of the Myxococcus xanthus gliding motor protein AglR, a homolog of the Escherichia coli flagella stator protein MotA. We observed that AglR decorated a helical structure, and the AglR helices rotated when cells were suspended in liquid or when cells moved on agar surfaces. With photoactivatable localization microscopy, we found that single molecules of AglR, unlike MotA/MotB, can move laterally within the membrane in helical trajectories. AglR slowed down transiently at gliding surfaces, accumulating in clusters. Our work shows that the untethered gliding motors of M. xanthus, by moving within the membrane, can transform helical motion into linear driving forces that push against the surface.
