Comparison of functional peptide encoded in the Escherichia coli 23S rRNA with other peptides involved in cis-regulation of translation

Biochem Cell Biol. 1995 Nov-Dec;73(11-12):1061-70. doi: 10.1139/o95-114.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Escherichia coli / genetics*
  • Genetic Code
  • Molecular Sequence Data
  • Peptides / genetics*
  • Protein Biosynthesis*
  • RNA, Bacterial / genetics*
  • RNA, Ribosomal, 23S / genetics*

Substances

  • Peptides
  • RNA, Bacterial
  • RNA, Ribosomal, 23S