Single base substitution in an intron of oxidase gene compensates splicing defects of the cytochrome b gene

Nature. 1982 Aug 12;298(5875):628-32. doi: 10.1038/298628a0.

Abstract

An extragenic suppressor mutation, mim2-1, which compensates yeast mitochondrial mutants deficient in splicing of the cytochrome b gene, has been mapped and sequenced. The mutation is due to a single G leads to A transition in the long open reading frame of the fourth intron of the oxidase subunit one gene. It causes the replacement of a glutamic codon by a lysine codon and the expression of a novel mRNA maturase active in splicing. Evolution and regulatory connections between homologous introns of nonhomologous genes are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Biological Evolution
  • Cytochrome b Group
  • Cytochromes / genetics*
  • DNA, Mitochondrial / genetics*
  • Electron Transport Complex IV / genetics*
  • Endonucleases / genetics*
  • Endoribonucleases*
  • Genes
  • Mutation
  • RNA Splicing*
  • Ribonucleases / genetics*
  • Saccharomyces cerevisiae / genetics
  • Suppression, Genetic

Substances

  • Cytochrome b Group
  • Cytochromes
  • DNA, Mitochondrial
  • Electron Transport Complex IV
  • Endonucleases
  • Endoribonucleases
  • Ribonucleases

Associated data

  • GENBANK/J01486