产气荚膜梭菌iota毒素和火鸡红细胞ADP-核糖基转移酶A对肌动蛋白的ADP-核糖基化作用：对原肌球蛋白调节的核苷酸交换和ATP酶活性的影响
ADP-ribosylation of actin by Clostridium perfringens iota toxin and turkey erythrocyte ADP-ribosyltransferase A: effects on profilin-regulated nucleotide exchange and ATPase activity.
作者信息
Sehr P, Just I, Aktories K
机构信息
Institut für Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, Germany.
出版信息
Naunyn Schmiedebergs Arch Pharmacol. 1996 Dec;354(6):693-7. doi: 10.1007/BF00166893.
Effects of ADP-ribosylation of skeletal muscle alpha-actin by Clostridium perfringens iota toxin and by turkey erythrocyte ADP-ribosyltransferase A on profilin-regulated nucleotide exchange and ATPase activity were compared. ADP-ribosylation of actin at Arg 177 by Clostridium perfringens iota toxin increased the nucleotide dissociation rate from 2.2 x 10(-3) s-1 to 4.5 x 10(-3) s-1 without affecting the profilin-induced stimulation of nucleotide exchange. In contrast, ADP-ribosylation of actin at Arg95/Arg372 induced by turkey erythrocyte transferase decreased the nucleotide dissociation rate to 1.5 x 10(3) s-1 and inhibited the profilin-induced stimulation of nucleotide exchange. Whereas toxin-induced ADP-ribosylation at Arg177 blocked actin ATPase, basal G-actin ATPase was not altered by ADP-ribosylation at Arg95/Arg372 but inhibited profilin effects on actin ATPase.
比较了产气荚膜梭菌iota毒素和火鸡红细胞ADP-核糖基转移酶A对骨骼肌α-肌动蛋白进行ADP-核糖基化作用，对原肌球蛋白调节的核苷酸交换和ATP酶活性的影响。产气荚膜梭菌iota毒素使肌动蛋白在精氨酸177位点发生ADP-核糖基化，核苷酸解离速率从2.2×10⁻³ s⁻¹增加到4.5×10⁻³ s⁻¹，且不影响原肌球蛋白诱导的核苷酸交换刺激作用。相反，火鸡红细胞转移酶诱导肌动蛋白在精氨酸95/精氨酸372位点发生ADP-核糖基化，使核苷酸解离速率降至1.5×10³ s⁻¹，并抑制原肌球蛋白诱导的核苷酸交换刺激作用。毒素诱导的精氨酸177位点ADP-核糖基化阻断了肌动蛋白ATP酶，而精氨酸95/精氨酸372位点的ADP-核糖基化未改变基础G-肌动蛋白ATP酶，但抑制了原肌球蛋白对肌动蛋白ATP酶的作用。
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