Purification of the RelB and RelE proteins of Escherichia coli:: RelE binds to RelB and to ribosomes

被引：47

作者：

Galvani, C ^{[1
]}

Terry, J ^{[1
]}

Ishiguro, EE ^{[1
]}

机构：

[1] Univ Victoria, Dept Biochem & Microbiol, Victoria, BC V8W 3P6, Canada

来源：

JOURNAL OF BACTERIOLOGY | 2001年 / 183卷 / 08期

关键词：

D O I：

10.1128/JB.183.8.2700-2703.2001

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The direct interaction of the Escherichia coli cytotoxin RelE,vith its specific antidote, RelB, was demonstrated in two ways: (i) copurification of the two proteins and (ii) a positive yeast two-hybrid assay involving the relB and relE genes. In addition, the purified RelE protein exhibited ribosome-binding activity in an in vitro assay, supporting previous observations suggesting that it is an inhibitor of translation.

引用

页码：2700 / 2703

页数：4

共 17 条

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