An E. coli aminoacyl-tRNA synthetase can substitute for yeast mitochondrial enzyme function in vivo

Cell. 1987 Nov 20;51(4):643-9. doi: 10.1016/0092-8674(87)90133-4.

Abstract

We have investigated the function of an E. coli aminoacyl-tRNA synthetase in S. cerevisiae strains that are respiration-deficient because of a mutation or a gene disruption in the nuclear encoded gene for the mitochondrial tyrosyl-tRNA synthetase. Although the yeast mitochondrial and E. coli tyrosine tRNAs differ significantly in sequence, expression of the E. coli tyrosyl-tRNA synthetase from a gene fusion restores respiration. The fusion gene contains a presumptive sequence for mitochondrial import from the mitochondrial tyrosyl-tRNA synthetase gene fused to the E. coli coding region. The fusion protein is incorporated into mitochondria. This incorporation and the rescue of the respiratory defect require the presumptive sequence for mitochondrial import. These experiments suggest a more limited definition of the identity of a tyrosine tRNA.

Publication types

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

MeSH terms

  • Amino Acyl-tRNA Synthetases / genetics
  • Amino Acyl-tRNA Synthetases / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Escherichia coli / enzymology*
  • Fungal Proteins
  • Genetic Complementation Test
  • Mitochondria / enzymology*
  • RNA, Fungal / metabolism
  • RNA, Transfer, Amino Acyl / metabolism
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae / enzymology*

Substances

  • Bacterial Proteins
  • Fungal Proteins
  • RNA, Fungal
  • RNA, Transfer, Amino Acyl
  • Recombinant Fusion Proteins
  • Amino Acyl-tRNA Synthetases