Evidence against tubulin oligomer dissociation to tubulin dimer at assembly temperatures.
Chromatography of microtubule protein through 8% agarose at 4 and 31 degrees C demonstrated that tubulin oligomer was not dissociated to tubulin dimer and microtubule associated proteins by assembly temperatures. During chromatography, formation of microtubules was prevented by using 10 microM podophyllotoxin and/or 25 microM GTP. In the presence of 25 microM GTP, tubulin oligomer at 31 degrees C and microtubule protein retained the ability to polymerize. Evidence against dimer formation from tubulin oligomer was also obtained via a turbidity study of the initial events (the first 90 s) of microtubule assembly.
D000818:Animals; D002417:Cattle; D002847:Chromatography, Agarose; D006160:Guanosine Triphosphate / Q000494:pharmacology; D066298:In Vitro Techniques; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism*; D011034:Podophyllotoxin / Q000494:pharmacology; D011487:Protein Conformation; D013696:Temperature; D014404:Tubulin / Q000302:isolation & purification / Q000378:metabolism*
D014404:Tubulin; D006160:Guanosine Triphosphate; D011034:Podophyllotoxin