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J. Biol. Chem., Vol. 269, Issue 50, 31338-31341, Dec, 1994
M Nakai, A Goto, T Nohara, D Sugita and T Endo
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.
Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport
Department of Chemistry, Faculty of Science, Nagoya University, Japan.
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