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  • Title: Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport.
    Author: Nakai M, Goto A, Nohara T, Sugita D, Endo T.
    Journal: J Biol Chem; 1994 Dec 16; 269(50):31338-41. PubMed ID: 7989297.
    Abstract:
    Recently, we identified the SecA and SecY proteins in the cyanobacterium Synechococcus PCC7942. Antibodies raised against cyanobacterial SecA specifically reacted with a 110-kDa protein of pea chloroplasts, suggesting the presence of SecA in higher plant chloroplasts. A part of the pea secA cDNA was polymerase chain reaction-amplified with degenerated oligonucleotide primers and with pea cDNA as a template. The deduced amino acid sequence shows 62% identity with cyanobacterial SecA and 52% identity with Escherichia coli SecA. Antibodies raised against the pea SecA fragment, which was expressed in E. coli cells from the obtained polymerase chain reaction-amplified cDNA, reacted with the 110-kDa chloroplast protein; the 110-kDa protein was mainly found in the stroma but partly in the thylakoid membrane. The anti-pea SecA IgG inhibited the in vitro import of the 33-kDa protein of the oxygen-evolving complex, but not of the 23-kDa protein of the oxygen-evolving complex, into thylakoids. These results suggest that SecA facilitates transport of a subset of thylakoid lumenal proteins including the 33-kDa protein into thylakoids. We propose that a bacterial-type Sec protein-dependent transport system operates for protein transport into thylakoids in higher plant chloroplasts.
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