Evidence of bar minigene expression and tRNA2Ile sequestration as peptidyl-tRNA2Ile during lambda bacteriophage development

J Bacteriol. 2004 Aug;186(16):5533-7. doi: 10.1128/JB.186.16.5533-5537.2004.

Abstract

Lambda bacteriophage development is impaired in Escherichia coli cells defective for peptidyl (pep)-tRNA hydrolase (Pth). Single-base-pair mutations (bar(-)) that affect translatable two-codon open reading frames named bar minigenes (barI or barII) in the lambda phage genome promote the development of this phage in Pth-defective cells (rap cells). When the barI minigene is cloned and overexpressed from a plasmid, it inhibits protein synthesis and cell growth in rap cells by sequestering tRNA(2)(Ile) as pep-tRNA(2)(Ile). Either tRNA(2)(Ile) or Pth may reverse these effects. In this paper we present evidence that both barI and barII minigenes are translatable elements that sequester tRNA(2)(Ile) as pep-tRNA(2)(Ile). In addition, overexpression of the barI minigene impairs the development even of bar(-) phages in rap cells. Interestingly, tRNA or Pth may reestablish lambda phage development. These results suggest that lambda bar minigenes are expressed and tRNA(2)(Ile) is sequestered as pep-tRNA(2)(Ile) during lambda phage development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteriophage lambda / genetics*
  • Bacteriophage lambda / growth & development*
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli / virology*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Escherichia coli Proteins / physiology
  • Genes, Viral*
  • Mutation
  • Open Reading Frames
  • Protein Biosynthesis
  • RNA, Transfer, Amino Acyl / biosynthesis
  • RNA, Transfer, Amino Acyl / metabolism*
  • RNA, Transfer, Ile / metabolism*

Substances

  • Escherichia coli Proteins
  • RNA, Transfer, Amino Acyl
  • RNA, Transfer, Ile
  • tRNA, peptidyl-
  • Carboxylic Ester Hydrolases
  • aminoacyl-tRNA hydrolase