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Volume 270, Number 28, Issue of July 14, pp. 16809-16812, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Colchicine Binding by the Isolated -Monomer of Tubulin

J. Wolff , Leslie Knipling

At mole ratios of lactoperoxidase to tubulin monomers of 3-4, bovine lactoperoxidase forms 1:1 adducts with both - and -tubulin from rat brain, thereby separating the tubulin heterodimer into its monomers. This mixture binds colchicine normally, and we show here by direct photoaffinity labeling that the bulk of the [H]colchicine becomes attached to -tubulin under these conditions. When the -tubulin has been displaced by lactoperoxidase, the ratio of label in -tubulin to -tubulin is increased. The amount of label in -tubulin decreases with a corresponding appearance of label in lactoperoxidase. The rate of labeling of -tubulin remains slow. We conclude that -tubulin is not necessary for colchicine binding and propose a model wherein the A and C rings of colchicine bind to -tubulin, while the B ring faces -tubulin in the dimer.

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