Cleavage of the precursor of pea chloroplast cytochrome f by leader peptidase from Escherichia coli.
Leader peptidase from Escherichia coli was able to process the precursor of pea cytochrome f synthesised in vitro. N-Terminal sequencing established that cleavage by leader peptidase generated the same mature sequence as in pea chloroplasts. Processing by leader peptidase was much more efficient co-translationally rather than post-translationally, and the extent of post-translational processing declined with time suggesting that the cytochrome f precursor folded to an uncleavable conformation. Detergent extracts of pea thylakoid membranes were unable to process the cytochrome f precursor co- or post-translationally.
Anderson
C M
CM
Botany School, University of Cambridge, UK.
Gray
J
J
D000595:Amino Acid Sequence; D002736:Chloroplasts / Q000201:enzymology*; D003580:Cytochromes / Q000235:genetics / Q000378:metabolism*; D045348:Cytochromes f; D010450:Endopeptidases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D007887:Fabaceae / Q000201:enzymology*; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010946:Plants, Medicinal; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases
D003580:Cytochromes; D008565:Membrane Proteins; D045348:Cytochromes f; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase