THE MAMMALIAN G-PROTEIN RHOC IS ADP-RIBOSYLATED BY CLOSTRIDIUM-BOTULINUM EXOENZYME C-3 AND AFFECTS ACTIN MICROFILAMENTS IN VERO CELLS
THE MAMMALIAN G-PROTEIN RHOC IS ADP-RIBOSYLATED BY CLOSTRIDIUM-BOTULINUM EXOENZYME C-3 AND AFFECTS ACTIN MICROFILAMENTS IN VERO CELLS
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DOI：
10.1002/j.1460-2075.1989.tb03477.x
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发表时间：
1989-04-01
期刊：
影响因子：
11.4
通讯作者：
GILL, DM
中科院分区：
文献类型：
--
作者：
CHARDIN, P;BOQUET, P;GILL, DM
肉毒梭菌C3是最近发现的一种外切酶，其ADP-核糖基化ras超家族的真核GTP结合蛋白。我们现在表明，人rhoC基因的细菌表达产物是ADP-核糖基化的C3和相应的大小，电荷和行为的占主导地位的C3基板的真核细胞。C3处理Vero细胞的结果在微丝的消失和辐射对称形状的变化没有任何明显的直接影响肌动蛋白。因此，ADP-核糖基化的rho蛋白似乎是负责微丝解体，我们推断，未经修改的形式的rho蛋白可能参与细胞骨架控制。
Clostridium botulinum C3 is a recently discovered exoenzyme that ADP-ribosylates a eukaryotic GTP-binding protein of the ras superfamily. We show now that the bacterially-expressed product of the human rhoC gene is ADP-ribosylated by C3 and corresponds in size, charge and behavior to the dominant C3 substrate of eukaryotic cells. C3 treatment of Vero cells results in the disappearance of microfilaments and in actinomorphic shape changes without any apparent direct effect upon actin. Thus the ADP-ribosylation of a rho protein seems to be responsible for microfilament disassembly and we infer that the unmodified form of a rho protein may be involved in cytoskeletal control.