The molecular mechanism of interaction of Et3Pb+ with tubulin

FEBS Letters

Faulstich, H.¹  Stournaras, C.¹  Doenges, K.H.²  Zimmermann, H.-P.² 

[1] Department of Physiology, Max-Planck-Institute for Medical Research, D-6900 Heidelberg, FRG;Institute of Cell and Tumor Biology, German Cancer Research Center, D-6900 Heidelberg, FRG

关键词: Triethyllead chloride;    Microtubule assembly;    Sulfhydryl group;    Disulfide;    Thiol reagents;    DTNB;    5;    5'-dithiobis(2-nitrobenzoic acid);    DNPSSG;    2;    4-dinitrophenylglutathionyl disulfide;    Et3Pb+;    triethyllead ion;    MAPs;    microtubule-associated proteins;   

DOI  :  10.1016/0014-5793(84)81090-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown