The leader peptides of attenuation-regulated chloramphenicol resistance genes inhibit translational termination.
Placing a translation stop codon at the ribosomal pause site in the leader of the attenuation-regulated cat-86 gene activates cat expression in the absence of the inducer, chloramphenicol. Genetic experiments have shown that this phenomenon depends on the amino acid sequence of the leader-encoded peptide and could readily be explained if the peptide was an inhibitor of translation termination. Here we demonstrate that the cat-86 leader pentapeptide is an in vitro inhibitor of translation termination in addition to its previously described antipeptidyltransferase activity.
Department of Biochemistry, University of Otago, Dunedin, New Zealand.
J G
JG
Moffat
W P
WP
Tate
P S
PS
Lovett
D000595:Amino Acid Sequence; D002702:Chloramphenicol Resistance / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial / Q000235:genetics; D008957:Models, Genetic; D008969:Molecular Sequence Data; D010443:Peptide Chain Termination, Translational / Q000187:drug effects*; D021382:Protein Sorting Signals / Q000494:pharmacology*; D012358:RNA, Transfer, Met / Q000378:metabolism
D021382:Protein Sorting Signals; D012358:RNA, Transfer, Met