PMID:8643630: Difference between revisions
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!align=left |Citation | |||
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'''Tenson, T, DeBlasio, A and Mankin, A''' (1996) A functional peptide encoded in the Escherichia coli 23S rRNA. ''Proc. Natl. Acad. Sci. U.S.A.'' '''93''':5641-6 | |||
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!align=left |Abstract | |||
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A pentapeptide open reading frame equipped with a canonical ribosome-binding site is present in the Escherichia coli 23S rRNA. Overexpression of 23S rRNA fragments containing the mini-gene renders cells resistant to the ribosome-inhibiting antibiotic erythromycin. Mutations that change either the initiator or stop codons of the peptide mini-gene result in the loss of erythromycin resistance. Nonsense mutations in the mini-gene also abolish erythromycin resistance, which can be restored in the presence of the suppressor tRNA, thus proving that expression of the rRNA-encoded peptide is essential for the resistance phenotype. The ribosome appears to be the likely target of action of the rRNA-encoded pentapeptide, because in vitro translation of the peptide mini-gene decreases the inhibitory action of erythromycin on cell-free protein synthesis. Thus, the new mechanism of drug resistance reveals that in addition to the structural and functional role of rRNA in the ribosome, it may also have a peptide-coding function. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8643630 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC39301 PMC39301] | |||
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| | !align=left |Keywords | ||
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|- | Amino Acid Sequence; Ampicillin Resistance; Base Sequence; Binding Sites; DNA Primers; DNA, Ribosomal/chemistry; DNA, Ribosomal/metabolism; Drug Resistance, Microbial; Erythromycin/pharmacology; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/metabolism; Genes, Suppressor; Molecular Sequence Data; Nucleic Acid Conformation; Open Reading Frames; Polymerase Chain Reaction; Protein Biosynthesis; RNA, Ribosomal, 23S/metabolism; Ribosomes/metabolism; Sequence Deletion | ||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
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==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:55, 15 September 2013
| Citation |
Tenson, T, DeBlasio, A and Mankin, A (1996) A functional peptide encoded in the Escherichia coli 23S rRNA. Proc. Natl. Acad. Sci. U.S.A. 93:5641-6 |
|---|---|
| Abstract |
A pentapeptide open reading frame equipped with a canonical ribosome-binding site is present in the Escherichia coli 23S rRNA. Overexpression of 23S rRNA fragments containing the mini-gene renders cells resistant to the ribosome-inhibiting antibiotic erythromycin. Mutations that change either the initiator or stop codons of the peptide mini-gene result in the loss of erythromycin resistance. Nonsense mutations in the mini-gene also abolish erythromycin resistance, which can be restored in the presence of the suppressor tRNA, thus proving that expression of the rRNA-encoded peptide is essential for the resistance phenotype. The ribosome appears to be the likely target of action of the rRNA-encoded pentapeptide, because in vitro translation of the peptide mini-gene decreases the inhibitory action of erythromycin on cell-free protein synthesis. Thus, the new mechanism of drug resistance reveals that in addition to the structural and functional role of rRNA in the ribosome, it may also have a peptide-coding function. |
| Links | |
| Keywords |
Amino Acid Sequence; Ampicillin Resistance; Base Sequence; Binding Sites; DNA Primers; DNA, Ribosomal/chemistry; DNA, Ribosomal/metabolism; Drug Resistance, Microbial; Erythromycin/pharmacology; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/metabolism; Genes, Suppressor; Molecular Sequence Data; Nucleic Acid Conformation; Open Reading Frames; Polymerase Chain Reaction; Protein Biosynthesis; RNA, Ribosomal, 23S/metabolism; Ribosomes/metabolism; Sequence Deletion |
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