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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >ADP-RIBOSYLATION OF ACTIN FROM THE GREEN ALGA CHARA CORALLINA BY CLOSTRIDIUM BOTULINUM C2 TOXIN AND CLOSTRIDIUM PERFRINGENS IOTA TOXIN
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ADP-RIBOSYLATION OF ACTIN FROM THE GREEN ALGA CHARA CORALLINA BY CLOSTRIDIUM BOTULINUM C2 TOXIN AND CLOSTRIDIUM PERFRINGENS IOTA TOXIN

机译：肉毒梭菌C2毒素和产气荚膜梭菌碘酒毒素对绿藻小球藻的ADP进行腺苷酸核糖化

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摘要

The ability of two bacterial toxins to modify a plant actin by covalent ADP-ribosylation was tested in the green alga Chara corallina. Using [P-32]NAD, both Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin labelled a protein of M(r) 42 kDa which comigrated with actin and was immunoprecipitated by a monoclonal anti-actin antibody. ADP-ribosylation of Chara actin was more efficient with iota toxin than with C2 toxin. The actin bundles in perfused Chara cells were not affected by toxin-containing media competent for ADP-ribosylation. The data indicate that monomeric plant actin is substrate for ADP-ribosylation by the bacterial toxins. [References: 36]
机译：在绿藻Chara Corallina中测试了两种细菌毒素通过共价ADP-核糖基化修饰植物肌动蛋白的能力。使用[P-32] NAD，肉毒梭菌C2毒素和产气荚膜梭状芽胞杆菌毒素都标记了M（r）42 kDa蛋白，该蛋白与肌动蛋白结合，并被单克隆抗肌动蛋白抗体免疫沉淀。 Chara肌动蛋白的ADP核糖基化使用Iota毒素比使用C2毒素更有效。灌注的Chara细胞中的肌动蛋白束不受主管ADP-核糖基化的含毒素培养基的影响。数据表明单体植物肌动蛋白是细菌毒素进行ADP-核糖基化的底物。 [参考：36]

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