Angela Berry


Hampton University / Pre-Pharmacy
Hosted by Zvonimir Dogic's Lab
The Nanometer-Scale Stepping Behaviors of Kinesin 401 and Kinesin 365
Angela Berry, Kun-Ta Wu, Zvonimir Dogic
Abstract: Kinesins are molecular motor proteins that move along microtubules in eukaryotic cells. Kinesin 401 is a processive molecular motor that has two legs walking on a microtubule, whereas Kinesin 365 is a non-processive motor that has one leg, therefore hopping on a microtubule. When assembled into kinesin clusters, these motors convert ATP into ADP, driving microtubule network. Kinesins promote intracellular activity, but the role of their nano-scale stepping behaviors in micron-scale network activity remains unclear. Here, we synthesize an active gel, a network comprised of crosslinked microtubules driven by molecular motor clusters. The clusters are comprised of kinesin motors crosslinked by streptavidin. We measured the network activity driven by kinesins 401and 365. Kinesin 365 reduces the molecular crowding of kinesin motors and microtubules. We found that kinesin 365 enhanced network activity, implying that non-processive motors drive the gel network more efficiently.
Our finding not only paves the way to outlining fundamental stepping behaviors of non-processive motors, but also sheds light on designing molecular motors that promote intracellular activity.
Support: MRSEC REU