Cross-hypersensitivity effects of mutations in 23 S rRNA yield insight into aminoacyl-tRNA binding

J Mol Biol. 1994 Nov 25;244(2):151-7. doi: 10.1006/jmbi.1994.1715.

Abstract

Halobacterium halobium cells contain one set of rRNA genes per genome. They have been used to characterize spontaneous mutants, carrying single nucleotide mutations in their rRNAs, that are resistant to different ribosomal antibiotics. Here we demonstrate that two different mutants that show resistance to thiostrepton, an inhibitor of the ribosomal GTPase-centre, are hypersensitive to amicetin, and other antibiotics, which act at the peptidyl transferase centre. Conversely, an amicetin-resistant mutant exhibits hypersensitivity to thiostrepton. A model is presented in which the two mutated sites, which are widely separated in the primary and secondary structure of 23 S rRNA, both participate in A-site binding of aminoacyl-tRNA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Base Sequence
  • Drug Resistance, Microbial / genetics*
  • Halobacterium salinarum / genetics*
  • Models, Genetic
  • Models, Molecular
  • Molecular Sequence Data
  • Point Mutation
  • Pyrimidine Nucleosides / pharmacology
  • RNA, Ribosomal, 23S*
  • RNA, Transfer, Amino Acyl / metabolism*
  • Thiostrepton / pharmacology

Substances

  • Anti-Bacterial Agents
  • Pyrimidine Nucleosides
  • RNA, Ribosomal, 23S
  • RNA, Transfer, Amino Acyl
  • amicetin
  • Thiostrepton