Cleavage of a synthetic COOH-terminal oligopeptide of D1 precursor protein by a purified processing enzyme.
A synthetic COOH-terminal oligopeptide of D1 protein deduced from the spinach psbA gene (Asn-325-Gly-353) was subjected to proteolytic digestion by purified processing enzyme of D1 protein [(1989) FEBS Lett. 246, 218-222] and the following two fragments were obtained as cleavage products: a COOH-terminal 9-amino-acid fragment (Ala-345-Gly-353) and an NH2-terminal 10-amino-acid fragment (Asn-325-Arg-334). It was concluded that: (i) the oligopeptide consisting of the COOH-terminal 29-amino-acid sequence deduced from the spinach psbA gene provides the recognition domain for the processing enzyme; (ii) the cleavage takes place at the predicted processing site of native D1 precursor protein (COOH side of Ala-344); and (iii) another cleavage takes place at an additional site (COOH side of Arg-334) for the synthetic substrate, but not for the native D1 precursor protein.
Fujita
S
S
Department of Biology, Faculty of Science, Okayama University, Japan.
Inagaki
N
N
Ono
T
T
Inoue
Y
Y
Satoh
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D002734:Chlorophyll / Q000235:genetics / Q000378:metabolism*; D005796:Genes; D045342:Light-Harvesting Protein Complexes; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism*; D014675:Vegetables
D000596:Amino Acids; D045342:Light-Harvesting Protein Complexes; D009842:Oligopeptides; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins; D011498:Protein Precursors; D002734:Chlorophyll; D010447:Peptide Hydrolases