Domain structure of mitochondrial and chloroplast targeting peptides

Eur J Biochem. 1989 Apr 1;180(3):535-45. doi: 10.1111/j.1432-1033.1989.tb14679.x.


Representative samples of mitochondrial and chloroplast targeting peptides have been analyzed in terms of amino acid composition, positional amino acid preferences and amphiphilic character. No highly conserved 'homology blocks' are found in either class of topogenic sequence. Mitochondrial-matrix-targeting peptides are composed of two domains with different amphiphilic properties. Arginine is frequently found either at position -10 or -2 relative to the cleavage site, suggesting that some targeting peptides may be cleaved twice in succession by two different matrix proteases. In stroma-targeting chloroplast transit peptides three distinct regions are evident: an uncharged amino-terminal domain, a central domain lacking acidic residues and a carboxy-terminal domain with the potential to form an amphiphilic beta-strand. Targeting peptides that route proteins to the mitochondrial intermembrane space or the lumen of chloroplast thylakoids have a mosaic design with an amino-terminal matrix- or stroma-targeting part attached to a carboxy-terminal extension that shares many characteristics with secretory signal peptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis*
  • Animals
  • Chloroplasts / analysis*
  • Humans
  • Hydrolysis
  • Mitochondria / analysis*
  • Molecular Structure
  • Peptide Fragments / analysis
  • Peptide Hydrolases
  • Peptides / analysis*
  • Plants
  • Protein Sorting Signals / analysis
  • Saccharomyces
  • Species Specificity


  • Amino Acids
  • Peptide Fragments
  • Peptides
  • Protein Sorting Signals
  • Peptide Hydrolases