Purification of the RelB and RelE Proteins of Escherichia coli: RelE Binds to RelB and to Ribosomes
AUTOR(ES)
Galvani, Cheryl
FONTE
American Society for Microbiology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=95192Documentos Relacionados
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