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Biochim Biophys Acta. 1991 Aug 23;1059(2):141-8.

Characterization of genes that encode subunits of cucumber PS I complex by N-terminal sequencing.

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Department of Chemistry, Meijo University, Nagoya, Japan.


N-terminal amino acid sequencing was carried out to characterize the genes of the cucumber PS I complex (PSI-100) that contains eight polypeptides and catalyzes the light-dependent transfer of electrons from plastocyanin to ferredoxin. The genes of all subunits except the 17.5 kDa polypeptide in PSI-100 have been identified. These are psaA/psaB (65/63 kDa), psaD (20 kDa), psaE (19.5 kDa), psaF (18.5 kDa), psaH (7.6 kDa), and psaC (5.8 kDa). The 17.5 kDa polypeptide is a new protein and is designated tentatively as the gene product of psaM. N-terminal amino-acid sequencing indicated the presence of two polypeptides in the 7.6 kDa band. One of these is the gene product of psaH and is essential for the activity of the PS I complex, and the other one is as yet unrecognized and largely depleted in the PSI-100 complex. Gene products of psaG, psaI, and psaK, which have been proposed as the components of PS I complex, are not involved in the PSI-100 complex, but are involved in the PS I complex (PSI-200), which contains 120 chlorophyll per reaction center chlorophyll (P700) and light-harvesting chlorophyll a/b protein complexes. Three polypeptides (26,23 and 22.5 kDa) are not involved in the PSI-100 and are assigned as the apo-protein of light-harvesting chlorophyll a/b protein complexes.

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