Abstract
A 25 kDa protein associated with Photosystem I (PS I) of the divinyl-chlorophyll a/b-containing oxychlorobacterium Prochlorococcus marinus SS120 (CCMP 1375) was isolated, and the amino acid sequences of the N-terminus and one internal peptide were determined. Polymerase chain reaction (PCR) with degenerate primers yielded a 92 bp fragment, which was used to isolate the complete gene from a genomic library. The corresponding gene was isolated from a library of Prochlorococcus sp. MED4 (CCMP 1378). In both Prochlorococcus strains, the gene encodes a protein of 199 amino acids. The gene products show a strong sequence similarity to the PS I subunit PsaL. The N-terminus contains a hydrophilic domain that has not been found in PsaL proteins from other organisms. In both strains, sequences encoding a protein similar to PsaI were found upstream of the psaL gene. Both genes are transcribed in the same direction.
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van der Staay, G.W., Moon-van der Staay, S.Y., Garczarek, L. et al. Characterization of the Photosystem I subunits PsaI and PsaL from two strains of the marine oxyphototrophic prokaryote Prochlorococcus. Photosynthesis Research 57, 183–191 (1998). https://doi.org/10.1023/A:1006098510768
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DOI: https://doi.org/10.1023/A:1006098510768