A cDNA clone encoding a photosystem I protein with homology to photosystem II chlorophyll a/b-binding polypeptides

We report here the isolation and nucleotide sequence of a complete cDNA clone encoding a photosystem I (PS I) polypeptide that is recognized by a monoclonal antibody made against photosystem II (PS II) chlorophyll a/b-binding (CAB) proteins. The deduced sequence of this PS I protein shows 30% overal...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1987-12, Vol.84 (24), p.8844-8848
Hauptverfasser: Hoffman, N.E, Pichersky, E, Malik, V.S, Castresana, C, Ko, K, Darr, S.C, Cashmore, A.R
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Sprache:eng
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Zusammenfassung:We report here the isolation and nucleotide sequence of a complete cDNA clone encoding a photosystem I (PS I) polypeptide that is recognized by a monoclonal antibody made against photosystem II (PS II) chlorophyll a/b-binding (CAB) proteins. The deduced sequence of this PS I protein shows 30% overall identity to PS II CAB sequences, and two long segments within this protein show 50% and 65% identity to the corresponding segments in the PS II CAB polypeptides. Even though the sequence of this PS I CAB protein is substantially divergent from PS II CAB sequences, their hydropathy plots are very similar and suggest they all traverse the thylakoid membrane three times. A segment of the PS I CAB polypeptide shows similarity to the functionally analogous β subunits of the antenna proteins of purple bacteria. In contrast, no homology was observed between these bacterial proteins and PS II CAB polypeptides.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.84.24.8844