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Cleavage of a synthetic COOH‐terminal oligopeptide of D1 precursor protein by a purified processing enzyme
Author(s) -
Fujita S.,
Inagaki N.,
Ono T.,
Inoue Y.,
Satoh K.
Publication year - 1989
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(89)81049-x
Subject(s) - oligopeptide , cleavage (geology) , chemistry , enzyme , terminal (telecommunication) , biochemistry , stereochemistry , peptide , biology , computer science , telecommunications , paleontology , fracture (geology)
A synthetic COOH‐terminal oligopeptide of D1 protein deduced from the spinach psb A 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 NH 2 ‐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 psb A gene provides the recognition domain for the processing enzyme; (ii) the cleavage takes place at the predicted processing site of native DI 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.