Difference in protein substrate specificity between hemorrhagic toxin and lethal toxin from Clostridium sordellii

被引：54
|
作者：
Genth, H [1 ]
Hofmann, F [1 ]
Selzer, J [1 ]
Rex, G [1 ]
Aktories, K [1 ]
Just, I [1 ]
机构：
[1] UNIV FREIBURG, INST PHARMAKOL & TOXIKOL, D-79104 FREIBURG, GERMANY
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1996年 / 229卷 / 02期
关键词：
D O I：
10.1006/bbrc.1996.1812
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The hemorrhagic toxin (HT) from Clostridium sordellii is pharmacologically related to Clostridium diffiicile toxins A and B and Clostridium sordellii lethal toxin which have been recently identified as mono-glucosyl-transferases. Here we report that HT, which is coexpressed with lethal toxin, is also a glucosyltransferase. Whereas lethal toxin glucosylates the Rho subfamily proteins Rac and Cdc42 and the Ras subfamily proteins H-Ras and Rap, the substrate specificity of HT is strictly confined to the Rho subfamily proteins Rho, Rac and Cdc42. Comparable to lethal toxin, transferase activity of HT is stimulated by Mn2+. Acceptor amino acid in Rho was identified by mutagenesis as threonine-37. C. sordellii HT is a novel member of the family of clostridial mono-glucosyl-transferases, a family which modifies the Rho and Ras GTPases. (C) 1996 Academic Press, Inc.
引用
收藏
页码：370 / 374
页数：5
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