Serrano L, Wandosell F, de la Torre J, Avila J
Centro de Biología Molecular (C.S.I.C.-U.A.M.), Universidad Autónoma, Madrid, Spain.
Biochem J. 1988 Jun 15;252(3):683-91. doi: 10.1042/bj2520683.
The capacity for self-polymerization and shape of the tubulin polymers assembled after digestion with trypsin, Pronase, chymotrypsin, subtilisin, Staphylococcus aureus proteinase V8 and proteinase K were investigated. Digestion with trypsin, Pronase or chymotrypsin resulted in a decrease in the ability of tubulin for self-assembly, whereas limited proteolysis with subtilisin, S. aureus proteinase V8 or proteinase K resulted in an increase in such ability. The shape of the assembled polymers varied from typical microtubules (after the treatment with trypsin or Pronase) to sheets (after the treatment with chymotrypsin) and from hooked microtubules with a constant polarity (after the treatment with subtilisin) to the disappearance of a defined polarity of such polymers (after the treatment with S. aureus V8 proteinase or proteinase K). These results indicate that the tubulin C-terminal regions are involved in the regulation of microtubule polymerization, shape, directional growth and lateral interactions between tubulin protofilaments.
研究了用胰蛋白酶、链霉蛋白酶、胰凝乳蛋白酶、枯草杆菌蛋白酶、金黄色葡萄球菌蛋白酶V8和蛋白酶K消化后组装的微管蛋白聚合物的自聚合能力和形状。用胰蛋白酶、链霉蛋白酶或胰凝乳蛋白酶消化导致微管蛋白的自组装能力下降，而用枯草杆菌蛋白酶、金黄色葡萄球菌蛋白酶V8或蛋白酶K进行有限的蛋白水解则导致这种能力增加。组装聚合物的形状从典型的微管（用胰蛋白酶或链霉蛋白酶处理后）到薄片（用胰凝乳蛋白酶处理后），从具有恒定极性的钩状微管（用枯草杆菌蛋白酶处理后）到此类聚合物明确极性的消失（用金黄色葡萄球菌V8蛋白酶或蛋白酶K处理后）。这些结果表明，微管蛋白C末端区域参与微管聚合、形状、定向生长以及微管蛋白原纤维之间横向相互作用的调节。
