Characterization of the Photosystem I subunits PsaI and PsaL from two strains of the marine oxyphototrophic prokaryote Prochlorococcus

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 deg...

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Veröffentlicht in:Photosynthesis research 1998-08, Vol.57 (2), p.183-191
Hauptverfasser: van der Staay, Georg Wm, Moon-van der Staay, Seung Yeo, Garczarek, Laurence, Partensky, Frédéric
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Sprache:eng
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Zusammenfassung: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.[PUBLICATION ABSTRACT]
ISSN:0166-8595
1573-5079
DOI:10.1023/A:1006098510768