Transport of proteins into chloroplasts. Partial purification of a chloroplast protease involved in the processing of important precursor polypeptides

Eur J Biochem. 1984 Jul 16;142(2):337-42. doi: 10.1111/j.1432-1033.1984.tb08291.x.


We have partially purified a soluble protease from Pisum sativum chloroplasts involved in the processing of precursor polypeptides imported into the organelle. The enzyme processes precursors of both stromal and thylakoid proteins to the mature size, but is inactive against all proteins so far tested other than precursors destined for the chloroplast. The enzyme processes precursors from wheat and barley, and is therefore not species-specific. It has a relative molecular mass of about 180 000 and a pH optimum near 9. The enzyme is inhibited by ethylenediamine tetraacetate and 1,10-phenanthroline but not by serine- or thiol-protease inhibitors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Transport
  • Chloroplasts / enzymology*
  • Edetic Acid / pharmacology
  • Fabaceae
  • Hydrogen-Ion Concentration
  • Molecular Weight
  • Peptide Hydrolases / isolation & purification
  • Peptide Hydrolases / metabolism*
  • Phenanthrolines / pharmacology
  • Plants, Medicinal
  • Plastocyanin / metabolism
  • Protease Inhibitors / pharmacology
  • Protein Precursors / metabolism*
  • Substrate Specificity


  • Phenanthrolines
  • Protease Inhibitors
  • Protein Precursors
  • Plastocyanin
  • Edetic Acid
  • Peptide Hydrolases
  • 1,10-phenanthroline