Tubulin carbamoylation. Functional amino groups in microtubule assembly.
The characteristics of the carbamoylation of pig brain tubulin were examined by using the modification conditions with cyanate described previously [Mellado, Slebe + Maccioni (1980) Biochem. Int. I, 584--590]. The carbamoylation reaction resulted in an inhibition of microtubule assembly, which was dependent on the concentration of the modifying agent. This tubulin modification appears to inhibit the growth of microtubules. The presence of GTP did not protect tubulin against this inhibition. Electron microscopy showed a marked decrease in the number of tubules after carbamoylation, but no alterations were observed in the microtubule morphology. The incorporation of KN14CO into alpha- and beta-subunits with similar kinetics was also shown, and the carbamoylated residues were identified as epsilon-N-carbamoyl-lysine residues.
D000818:Animals; D001665:Binding Sites; D001704:Biopolymers; D001923:Brain Chemistry; D003078:Colchicine / Q000378:metabolism; D003485:Cyanates / Q000494:pharmacology; D006160:Guanosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D008854:Microscopy, Electron; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D013552:Swine; D014404:Tubulin / Q000378:metabolism*
D001704:Biopolymers; D003485:Cyanates; D014404:Tubulin; D006160:Guanosine Triphosphate; C024835:potassium cyanate; D003078:Colchicine