Isolation and characterization of the cDNA for pea chloroplast SecA Evolutionary conservation of the bacterial‐type SecA‐dependent protein transport within chloroplasts

FEBS Letters

Nohara, Tetsuya¹  Nakai, Masato¹  Goto, Akira¹  Endo, Toshiya¹ 

[1] Department of Chemistry, Faculty of Science, Nagoya University Chikusa-ku, Nagoya 464-01, Japan

关键词: SecA;    Chloroplast;    Protein import;    Thylakoid;    E. coli;    Escherichia coli;    DHFR;    dihydrofolate reductase;    S(1–129)-DHFR;    a fusion protein consisting of residues 1–129 of pea SecA followed by DHFR;    S(62–129)-DHFR;    a fusion protein consisting of residues 62–129 of pea SecA followed by DHFR;    SecA(1–303);    a truncated protein corresponding to residues 1–303 of pea SecA;    33K;    33-kDa protein of the pea photosystem II oxygen-evolving complex;    NiߜNTA;    Niߜnitriloߜtriacetic acid;   

DOI  :  10.1016/0014-5793(95)00415-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We report here the isolation of the cDNA for pea chloroplast SecA. Pea SecA encodes a polypeptide of 1,011 amino acids and shows high sequence similarity with cyanobacterial SecA. Pea SecA was synthesized as a larger precursor and was imported into isolated chloroplasts in vitro. The purified pea SecA, which was expressed in Escherichia coli cells, stimulated the in vitro import of the 33 kDa protein of the oxygen-evolving complex into thylakoids. These results indicate that higher plant chloroplasts contain a bacterial-type SecA protein-dependent system for the intraorganellar protein transport into thylakoids.

【 授权许可】

Unknown