The molecular mechanism of interaction of Et3Pb+ with tubulin

Faulstich, Heinz; Stournaras, Christos; Doenges , K.H.; Zimmermann, H.-P.

doi:10.1016/0014-5793(84)81090-X

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The molecular mechanism of interaction of Et3Pb+ with tubulin

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Faulstich, Heinz
Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society;

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Stournaras, Christos
Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Faulstich, H., Stournaras, C., Doenges, K., & Zimmermann, H.-P. (1984). The molecular mechanism of interaction of Et3Pb+ with tubulin. FEBS Letters, 174(1), 128-131. doi:10.1016/0014-5793(84)81090-X.

Cite as: https://hdl.handle.net/21.11116/0000-0006-8B67-A

Abstract

Triethyllead ion (Et3Pb+) was found to interact with 2 out of 18 thiol groups present in tubulin dimers. Specificity of the interaction was shown by the high affinity of Et3Pb+ to tubulin, by the fact that the 16 residual thiol groups in tubulin remained unaffected, and by the observation that other proteins with exposed thiol groups, e.g., actin, did not react with Et3Pb+. After complexation of the two thiol groups, tubulin in vitro had lost its capability for microtubule assembly. Likewise, polymerized tubulin disassembled on addition of the lead compound.