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The molecular mechanism of interaction of Et 3 Pb + with tubulin
Author(s) -
Faulstich H.,
Stournaras C.,
Doenges K.H.,
Zimmermann H.-P.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81090-x
Subject(s) - tubulin , mechanism (biology) , chemistry , biophysics , physics , microtubule , biology , genetics , quantum mechanics
Triethyllead ion (Et 3 Pb + ) 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 Et 3 Pb + 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 Et 3 Pb + . 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.