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Cleavage of the precursor of pea chloroplast cytochrome ƒ by leader peptidase from Escherichia coli
Author(s) -
Anderson Clare M.,
Gray John
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80337-3
Subject(s) - escherichia coli , chloroplast , thylakoid , cleavage (geology) , biochemistry , cytochrome , cytochrome c , cytochrome f , biology , protein precursor , signal peptidase , chemistry , peptide sequence , enzyme , signal peptide , gene , mitochondrion , paleontology , fracture (geology)
Leader peptidase from Escherichia coli was able to process the precursor of pea cytochrome ƒ 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 ƒ precursor folded to an uncleavable conformation. Detergent extracts of pea thylakoid membranes were unable to process the cytochrome ƒ precursor co‐ or post‐translationally.