Mutations in the rpmBG operon of Escherichia coli that affect ribosome assembly

J Bacteriol. 1997 Apr;179(8):2486-93. doi: 10.1128/jb.179.8.2486-2493.1997.

Abstract

The rpmBG operon of Escherichia coli codes for ribosomal proteins L28 and L33. Two strains with mutations in the operon are AM81, whose ribosomes lack protein L28, and AM90, whose ribosomes are without protein L33. Neither strain showed major defects in ribosome assembly. However, when the mutations were transferred to other strains of E. coli, ribosome synthesis was greatly perturbed and precursor ribonucleoproteins accumulated. In the new backgrounds, the mutation in rpmB was complemented by synthesis of protein L28 from a plasmid; the rpmG mutation was not complemented by protein L33 because synthesis of protein L28 from the upstream rpmB gene was also greatly reduced. The results suggest that protein L33, in contrast to protein L28, has at best a minor role in ribosome assembly and function.

MeSH terms

  • Amino Acid Sequence
  • Aniline Compounds*
  • Bacterial Proteins*
  • Base Sequence
  • Escherichia coli / genetics*
  • Escherichia coli Proteins*
  • Frameshift Mutation
  • Genetic Complementation Test
  • Molecular Sequence Data
  • Mutation / genetics*
  • Operon / genetics
  • Phenotype
  • Ribosomal Proteins / biosynthesis
  • Ribosomal Proteins / genetics*
  • Ribosomes / metabolism*
  • Sequence Analysis
  • Species Specificity
  • Suppression, Genetic
  • Transduction, Genetic

Substances

  • Aniline Compounds
  • Bacterial Proteins
  • Escherichia coli Proteins
  • L33 ribosomal protein, bacteria
  • Ribosomal Proteins
  • rpmB protein, E coli
  • rpmG protein, E coli
  • 4-trifluoromethylaniline