Carlier M F, Didry D, Pantaloni D
Laboratoire d'Enzymologie et Biochimie Structurale, CNRS, Gif-sur-Yvetta, France.
Biophys J. 1997 Jul;73(1):418-27. doi: 10.1016/S0006-3495(97)78081-0.
Hydrolysis of GTP is known to accompany microtubule assembly. Here we show that hydrolysis of GTP is also associated with the formation of linear oligomers of tubulin, which are precursors (prenuclei) in microtubule assembly. The hydrolysis of GTP on these linear oligomers inhibits the lateral association of GTP-tubulin that leads to the formation of a bidimensional lattice. Therefore GTP hydrolysis interferes with the nucleation of microtubules. Linear oligomers are also formed in mixtures of GTP-tubulin and GDP-tubulin. The hydrolysis of GTP associated with heterologous interactions between GTP-tubulin and GDP-tubulin in the cooligomer takes place at a threefold faster rate than upon homologous interactions between GTP-tubulins. The implication of these results in a model of vectorial GTP hydrolysis in microtubule assembly is discussed.
已知GTP水解伴随着微管组装过程。在此我们表明,GTP水解还与微管蛋白线性寡聚体的形成相关,这些线性寡聚体是微管组装的前体(前核)。这些线性寡聚体上GTP的水解抑制了GTP-微管蛋白的侧向缔合,而这种侧向缔合会导致二维晶格的形成。因此,GTP水解会干扰微管的成核过程。线性寡聚体也会在GTP-微管蛋白和GDP-微管蛋白的混合物中形成。与共聚物中GTP-微管蛋白和GDP-微管蛋白之间的异源相互作用相关的GTP水解速率,比GTP-微管蛋白之间的同源相互作用时快三倍。本文讨论了这些结果对微管组装中矢量GTP水解模型的意义。