肌动蛋白的ADP核糖基化导致ATP交换速率增加并抑制ATP水解。
ADP-ribosylation of actin causes increase in the rate of ATP exchange and inhibition of ATP hydrolysis.
作者信息
Geipel U, Just I, Schering B, Haas D, Aktories K
机构信息
Rudolf-Buchheim-Institut für Pharmakologie, Justus-Liebig-Universität Giessen, Federal Republic of Germany.
出版信息
Eur J Biochem. 1989 Jan 15;179(1):229-32. doi: 10.1111/j.1432-1033.1989.tb14545.x.
ADP-ribosylation of skeletal muscle actin by Clostridium perfringens iota toxin increased the rate of exchange of actin-bound [gamma-32P]ATP by unlabelled ATP about twofold. Increased exchange rates were observed with ATP and ATP[gamma S], much less with ADP but not with AMP or NAD. ADP-ribosylation of skeletal muscle actin reduced "basal" and Mg2+ (1 mM)-induced ATP hydrolysis by about 80%. Similar inhibition of ATP hydrolysis was observed with liver actin ADP-ribosylated by Clostridium botulinum C2 toxin. The data indicate that ADP-ribosylation of actin at Arg-177 largely affects the ATP-binding and ATPase activity.
产气荚膜梭菌iota毒素对骨骼肌肌动蛋白的ADP核糖基化作用使肌动蛋白结合的[γ-32P]ATP与未标记ATP的交换速率提高了约两倍。ATP和ATP[γS]可使交换速率增加，ADP的作用则小得多，而AMP或NAD则无此作用。骨骼肌肌动蛋白的ADP核糖基化使“基础”和Mg2+（1 mM）诱导的ATP水解降低了约80%。肉毒梭菌C2毒素对肝脏肌动蛋白进行ADP核糖基化时也观察到了类似的ATP水解抑制作用。数据表明，肌动蛋白在Arg-177处的ADP核糖基化在很大程度上影响了ATP结合和ATP酶活性。
Zotero 插件