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

Authors
Galvani, C Terry, J Ishiguro, EE
Citation
C. Galvani et al., Purification of the RelB and RelE proteins of Escherichia coli: RelE bindsto RelB and to ribosomes, J BACT, 183(8), 2001, pp. 2700-2703
Citations number
17
Categorie Soggetti
Microbiology
Journal title
JOURNAL OF BACTERIOLOGY
ISSN journal
00219193 → ACNP
Volume
183
Issue
8
Year of publication
2001
Pages
2700 - 2703
Database
ISI
SICI code
0021-9193(200104)183:8<2700:POTRAR>2.0.ZU;2-X
Abstract
The direct interaction of the Escherichia coli cytotoxin RelE,vith its spec ific antidote, RelB, was demonstrated in two ways: (i) copurification of th e two proteins and (ii) a positive yeast two-hybrid assay involving the rel B and relE genes. In addition, the purified RelE protein exhibited ribosome -binding activity in an in vitro assay, supporting previous observations su ggesting that it is an inhibitor of translation.