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Coming Events

10/24/2014 - Partners in Giving - Popcorn Extravaganza
10/24/2014 - IPiB Seminar Series - Brendan Floyd
10/27/2014 - Contemporary Biochemistry - Paul Selvin

Rayment Lab - When is a motor not a motor?
A Kinesin Motor without a Nucleotide Binding Site

It is widely accepted that kinesin molecular motors contain a motor domain that hydrolyzes ATP and through a series of nucleotide-dependent conformational changes translate the free energy of hydrolysis into directed movement. Thus it comes as a complete surprise that the kinesin related protein Vik1 contains a motor domain, but does not include an active site. This non-motor polypeptide heterodimerizes with the kinesin Kar3. Surprisingly, Vik1 can bind tightly to microtubules independently of Kar3, but still permits movement of Kar3 along microtubules. These traits demand that there is communication between Kar3 and Vik1, perhaps through a novel strain-dependent mechanism, that allows the binding affinity of Vik1 for microtubules to be modulated by the nucleotide state of Kar3. From an evolutionary viewpoint it is appears that Vik1 evolved from a primordial gene belonging to the same kinesin family as Kar3. Remarkably, the ability to bind and hydrolyze nucleotide was lost during evolution, but the ability to interact with microtubules and communicate with its associated motor protein Kar3 was retained. These studies suggest new variations of molecular motor interactions await discovery.

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