The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site.
Cell
; 112(1): 131-40, 2003 Jan 10.
Article
en En
| MEDLINE
| ID: mdl-12526800
ABSTRACT
The Escherichia coli relBE operon encodes a toxin-antitoxin pair, RelE-RelB. RelB can reverse inhibition of protein synthesis by RelE in vivo. We have found that although RelE does not degrade free RNA, it cleaves mRNA in the ribosomal A site with high codon specificity. Among stop codons UAG is cleaved with fast, UAA intermediate and UGA slow rate, while UCG and CAG are cleaved most rapidly among sense codons. We suggest that inhibition of protein synthesis by RelE is reversed with the help of tmRNA, and that RelE plays a regulatory role in bacteria during adaptation to poor growth conditions.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Ribosómicas
/
Toxinas Bacterianas
/
Codón
/
ARN Mensajero
/
Proteínas de Escherichia coli
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Cell
Año:
2003
Tipo del documento:
Article
País de afiliación:
Dinamarca