Comparison of functional peptide encoded in the Escherichia coli 23S rRNA with other peptides involved in cis-regulation of translation.
A new approach for studying functional rRNA fragments has been developed based on using a plasmid library expressing random fragments of rRNA. A 34 nucleotide long fragment of Escherichia coli 23S rRNA has been identified that renders cells resistant to erythromycin, when expressed in vivo. The rRNA fragment contains a five codon long open reading frame, initiating at GUG and terminating at UAA, with a Shine-Dalgarno sequence located at an appropriate distance from the initiator codon. Translation of this mini-gene is required for the observed erythromycin resistance. Experiments with in vitro translated, or synthetic, peptide indicate the ribosome as a likely target for the action of the identified rRNA-encoded peptide, which apparently remains associated with the ribosome after completion of its translation. The known properties of the rRNA-encoded peptide are compared with information about other functionally active short peptides that can be involved in regulation of translation.
Tenson
T
T
Center for Pharmaceutical Biotechnology, University of Illinois, Chicago, IL 60612, USA.
Mankin
A
A
D000595:Amino Acid Sequence; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics*; D005815:Genetic Code; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics*; D014176:Protein Biosynthesis; D012329:RNA, Bacterial / Q000235:genetics*; D012338:RNA, Ribosomal, 23S / Q000235:genetics*
D010455:Peptides; D012329:RNA, Bacterial; D012338:RNA, Ribosomal, 23S