ISOLATION AND CHARACTERIZATION OF THE CDNA FOR PEA CHLOROPLAST SECA EVOLUTIONARY CONSERVATION OF THE BACTERIAL-TYPE SECA-DEPENDENT PROTEIN-TRANSPORT WITHIN CHLOROPLASTS
T. Nohara et al., ISOLATION AND CHARACTERIZATION OF THE CDNA FOR PEA CHLOROPLAST SECA EVOLUTIONARY CONSERVATION OF THE BACTERIAL-TYPE SECA-DEPENDENT PROTEIN-TRANSPORT WITHIN CHLOROPLASTS, FEBS letters, 364(3), 1995, pp. 305-308
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 sequen
ce 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-ev
olving complex into thylakoids, These results indicate that higher pla
nt chloroplasts contain a bacterial-type SecA protein-dependent system
for the intraorganellar protein transport into thylakoids.