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Transport of proteins into chloroplasts partial purification of a chloroplast protease involved in the processing of imported precursor polypeptides

, : Transport of proteins into chloroplasts partial purification of a chloroplast protease involved in the processing of imported precursor polypeptides. European Journal of Biochemistry 142(2): 337-342

A soluble protease from Pisum sativum chloroplasts involved in the processing of precursor polypeptides imported into the organelle was partially purified. 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 .apprx. 180,000 and a pH optimum near 9. The enzyme is inhibited by EDTA and 1,10-phenanthroline but not by serine- or thiol-protease inhibitors.


DOI: 10.1111/j.1432-1033.1984.tb08291.x

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