A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles

Article Abstract:

A new kinesin protein has been discovered that is also a microtubule-dependent motor enzyme participating in mitosis. The new protein was first described as a spindle antigen necessary for mitotic progression. The cloning of this protein's gene revealed a resemblance to the motor domain of kinesin-like proteins. The protein is able to cross-bridge antiparallel microtubules in vitro and to assist the microtubules in sliding over each other as must occur for spindles to elongate.

Enzymes, Mitosis, Spindle (Cell division), Spindle (Cytoplasm)

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Minus-end directed motion of kinesin-coated microspheres driven by microtubule depolymerization

Article Abstract:

The in vitro movement of latex microsphere on disassembling microtubules (MTs) is facilitated by several enzymes such as kinesin. Dynamic variations in MT length results in intracellular motility. The in vitro movement is investigated in the lysed Tetrahymena species, which exhibits disassembly-dependent movement of chromosomes. The MT disassembly possesses the ability to reverse the polarity of kinesin's motor activity and influences the rate of depolymerization of tubulin.

Kinesin, Latex

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Force production by disassembling microtubules

Article Abstract:

Depolymerizing microtubules (MT) exert a brief tug on the beads as measured with laser tweezers when conjugating glass microbeads to tubulin polymers through strong inert linkages. Interactions with a molecular-mechanical model of MT structure and force production a single depolymerizing MT generates about ten times the force developed by a motor enzyme, thus the mechanism is the primary driving force for chromosome motion.

United States, Science & research, Physiological aspects, Genetic aspects, Eukaryotes, Thin layer chromatography, Structure

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