1. Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs
- Author
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Pushpanjali Soppina, Nishaben Patel, Dipeshwari J. Shewale, Ashim Rai, Sivaraj Sivaramakrishnan, Pradeep K. Naik, and Virupakshi Soppina
- Subjects
Chemomechanical ,Kinesin-3 ,Microtubule bending ,Baculovirus ,Superprocessive ,ATPases ,Biology (General) ,QH301-705.5 - Abstract
Abstract Background Kinesin-3 family motors drive diverse cellular processes and have significant clinical importance. The ATPase cycle is integral to the processive motility of kinesin motors to drive long-distance intracellular transport. Our previous work has demonstrated that kinesin-3 motors are fast and superprocessive with high microtubule affinity. However, chemomechanics of these motors remain poorly understood. Results We purified kinesin-3 motors using the Sf9-baculovirus expression system and demonstrated that their motility properties are on par with the motors expressed in mammalian cells. Using biochemical analysis, we show for the first time that kinesin-3 motors exhibited high ATP turnover rates, which is 1.3- to threefold higher compared to the well-studied kinesin-1 motor. Remarkably, these ATPase rates correlate to their stepping rate, suggesting a tight coupling between chemical and mechanical cycles. Intriguingly, kinesin-3 velocities (KIF1A > KIF13A > KIF13B > KIF16B) show an inverse correlation with their microtubule-binding affinities (KIF1A
- Published
- 2022
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