Functional evidence for indirect recognition of G.U in tRNA(Ala) by alanyl-tRNA synthetase

Science. 1996 Jan 12;271(5246):195-7. doi: 10.1126/science.271.5246.195.

Abstract

The structural features of the G.U wobble pair in Escherichia coli alanine transfer RNA (tRNA(Ala)) that are associated with aminoacylation by alanyl-tRNA synthetase (AlaRS) were investigated in vivo for wild-type tRNA(Ala) and mutant tRNAs with G.U substitutions. tRNA(Ala) with G.U, C.A, or G.A gave similar amounts of charged tRNA(Ala) and supported viability of E. coli lacking chromosomal tRNA(Ala) genes. tRNA(Ala) with G.C was inactive. Recognition of G.U by AlaRS thus requires more than the functional groups on G.U in a regular helix and may involve detection of a helical distortion.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alanine-tRNA Ligase / metabolism*
  • Anticodon
  • Base Composition
  • Base Sequence
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Genes, Bacterial
  • Guanine / chemistry
  • Molecular Sequence Data
  • Mutation
  • Nucleic Acid Conformation
  • Plasmids
  • RNA, Transfer, Ala / chemistry
  • RNA, Transfer, Ala / genetics
  • RNA, Transfer, Ala / metabolism*
  • Uracil / chemistry

Substances

  • Anticodon
  • RNA, Transfer, Ala
  • Uracil
  • Guanine
  • Alanine-tRNA Ligase