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'Prima donna' protein doesn't work well in pairs
Date:11/5/2010

"Our analyses show that the two kinesins must stay in close proximity to one another to cooperate effectively," he said. "Otherwise, one of the motors will tend to assume all of the applied force imposed on the cargo. Kinesin is relatively fast and efficient on its own, but they have trouble keeping up with one another when they are connected together."

Diehl said the group suspects that other classes of motor molecules, which are somewhat weaker than kinesin, may function better in groups. The team is carrying out follow-up experiments to see if that's the case, and they are examining how such distinctions may play a role in regulating cargo movement in cells.

Diehl's research group, which is located in Rice's new BioScience Research Collaborative, has spent years refining the tools used in the new study, and the work is paying off in numerous ways. Within the past four months, the group won an R01 grant from the National Institutes of Health worth more than $1.4 million, and Diehl also published a theoretical study of motor proteins with Rice chemist Anatoly Kolomeisky.


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Contact: Jade Boyd
jadeboyd@rice.edu
713-348-6778
Rice University
Source:Eurekalert  

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