A mutant of the motor protein kinesin that moves in both directions on microtubules
Article Abstract:
Research is presented concerning the amino-acid changes at the Ncd neck which influence the direction of travel of molecular motors to the minus or plus end of actin filaments or microtubules.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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Self-organization of microtubules and motors
Article Abstract:
Researchers constructed a simple system of microtubules and molecular motors to investigate the self-organization process in cellular structure. They observed the production of asters both within a system comprising only stabilized microtubules and multi-headed constructs of the motor protein kinesin, and also from a homogenous solution of motors and tubulin. They also obtained a range of self-organized structures by changing the relative concentrations of the components, and when they studied the process in a micro-fabricated glass chamber.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Decoupling of nucelotide- and microtubule-binding sites in a kinesin mutant
Article Abstract:
A mutation in the motor domain of the motor proteins Kar3 and Ncd is found to uncouple nucleotide- and microtubule-binding by proteins. This prevents activation of the motor ATPase by microtubules. Mutants are tightly bound to ADP and microtubules, suggesting a blockage of interactions between the nucleotide and microtubule binding sites. The area incorporating the mutated amino acid may transmit or change in order to conver the motor ATPase.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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