The molecular mechanism of interaction of Et3Pb+ with tubulin.
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.
D000199:Actins / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000378:metabolism; D007854:Lead / Q000494:pharmacology*; D046911:Macromolecular Substances; D008870:Microtubules / Q000378:metabolism / Q000648:ultrastructure; D009132:Muscles / Q000378:metabolism; D009498:Neurotoxins / Q000494:pharmacology*; D009942:Organometallic Compounds / Q000494:pharmacology*; D011485:Protein Binding; D011817:Rabbits; D013552:Swine; D014404:Tubulin / Q000378:metabolism*
D000199:Actins; D046911:Macromolecular Substances; D009498:Neurotoxins; D009942:Organometallic Compounds; D014404:Tubulin; D007854:Lead; C010360:triethyllead