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Erythromycin resistance peptides selected from random peptide libraries

T Tenson1, L Xiong, P Kloss

  • 1Center for Pharmaceutical Biotechnology, University of Illinois, Chicago, Illinois 60607-7173, USA.

The Journal of Biological Chemistry
|July 11, 1997
PubMed
Summary

Short peptides translated from Escherichia coli 23S ribosomal RNA (rRNA) can confer antibiotic resistance. These peptides interact with the ribosome, offering insights into peptide binding sites and mechanisms of action for macrolide antibiotics.

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Area of Science:

  • Molecular Biology
  • Microbiology
  • Biochemistry

Background:

  • Previous studies demonstrated that a 5-codon mini-gene in Escherichia coli 23S ribosomal RNA (rRNA) confers erythromycin resistance.
  • This resistance is mediated by the specific interaction of the 23S rRNA-encoded pentapeptide with the ribosome.

Purpose of the Study:

  • To investigate the structural features of peptides that confer erythromycin resistance.
  • To identify peptides with antibiotic resistance activity using in vivo expressed random peptide libraries.

Main Methods:

  • Screening of a 21-codon mini-gene library (ATG (NNN)20 TAA) to identify peptides conferring erythromycin resistance.
  • Sequence comparison of resistance peptides from a 5-codon library (ATG (NNN)4 TAA).
  • Testing the erythromycin resistance peptides against other antibiotics, including macrolides, oleandomycin, spiramycin, chloramphenicol, and clindamycin.

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Main Results:

  • Only short peptides, 3-6 amino acids long, conferred erythromycin resistance.
  • A strong preference was observed for leucine or isoleucine at the third amino acid position and a hydrophobic amino acid at the C-terminus.
  • The identified peptides conferred resistance to other macrolides (oleandomycin, spiramycin) but not to chloramphenicol or clindamycin.

Conclusions:

  • Defining the consensus amino acid sequence of these peptides provides insights into their mode of action.
  • The findings suggest a specific peptide binding site on the ribosome involved in antibiotic resistance.