Cleavage of a synthetic COOH‐terminal oligopeptide of D1 precursor protein by a purified processing enzyme

FEBS Letters

Inoue, Y.²  Inagaki, N.¹  Satoh, K.¹  Ono, T.²  Fujita, S.¹ 

[1] Department of Biology, Faculty of Science, Okayama University, Okayama 700 Japan;Solar Energy Research Group, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01, Japan

关键词: Protein;    D1;    Enzyme;    processing;    Gene;    psbA;    Photosystem II;    Reaction center;    Oligopeptide;    synthetic;    HPLC;    high-performance liquid chromatography;    TFA;    trifluoroacetic acid;    PS;    photosystem;   

DOI  :  10.1016/0014-5793(89)81049-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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.

【 授权许可】

Unknown