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PMID: 11274135 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Journal of bacteriology ·Vol. 183 ·No. 8 ·2001-04-00 ·Pages 2700-3

Galvani C, Terry J, Ishiguro EE

Abstract

The direct interaction of the Escherichia coli cytotoxin RelE with 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.

MeSH Terms
Antitoxins/genetics,isolation & purification,metabolism Bacterial Toxins/genetics,isolation & purification,metabolism,toxicity Cytotoxins/genetics,isolation & purification,metabolism,toxicity Escherichia coli/genetics,metabolism Proto-Oncogene Proteins/genetics,isolation & purification,metabolism Ribosomes/metabolism Transcription Factor RelB Transcription Factors/genetics,isolation & purification,metabolism Two-Hybrid System Techniques
Chemicals
Antitoxins Bacterial Toxins Cytotoxins Proto-Oncogene Proteins Transcription Factors Transcription Factor RelB
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Galvani C
Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada.
Terry J
Ishiguro E E
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13 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.183.8.2700-2703.2001
Published
2001-04-00
Pages
2700-3
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC95192
Subset
IM
External Links
PubMed source DOI: 10.1128/JB.183.8.2700-2703.2001 PMC Full Text View journal details
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