The carboxy-terminal end of glycolate oxidase directs a foreign protein into tobacco leaf peroxisomes

Plant J. 1991 Nov;1(3):361-6. doi: 10.1046/j.1365-313x.1991.t01-4-00999.x.


The carboxy-terminal residues of several peroxisomal proteins were shown to act as a peroxisomal targetting signal. This study was conducted to test whether the C-terminus of glycolate oxidase, a key enzyme in the glycolate metabolism pathway, is functioning as a targetting signal that directs proteins into plant leaf peroxisomes. A chimeric gene coding for a fusion protein composed of the C-terminal-truncated beta-glucuronidase, a synthetic linker of four amino acids and the last six C-terminal amino acids of glycolate oxidase, was constructed. Transformation of tobacco plants with the chimeric gene resulted in expression of beta-glucuronidase enzymic activity. About 50% of the transgenic beta-glucuronidase activity was localized to the peroxisomes. The results indicate that the six C-terminal amino acid residues of glycolate oxidase act as a targetting signal that is recognized by leaf peroxisomes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / genetics
  • Alcohol Oxidoreductases / metabolism*
  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • DNA / genetics
  • Gene Expression
  • Glucuronidase / genetics
  • Glucuronidase / metabolism
  • Microbodies / metabolism
  • Molecular Sequence Data
  • Plant Proteins / metabolism*
  • Plants / genetics
  • Plants / metabolism*
  • Plants, Toxic
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Subcellular Fractions / metabolism
  • Tobacco / genetics
  • Tobacco / metabolism


  • Plant Proteins
  • Recombinant Fusion Proteins
  • DNA
  • Alcohol Oxidoreductases
  • glycollate oxidase
  • Glucuronidase