Mutational Analysis of the Structure and Biogenesis of the Photosystem I Reaction Center in the Cyanobacterium Synechocystis sp. PCC 6803

We have utilized the unicellular cyanobacterium Synechocystis sp. PCC 6803 to incorporate site-directed amino acid substitutions into the photosystem I (PSI) reactioncenter protein PsaB. A cysteine residue (position 565 of PsaB) proposed to serve as a ligand to the [4Fe-4S] center Fxwas changed to s... Ausführliche Beschreibung

Quelle: in Proceedings of the National Academy of Sciences of the United States of America Vol. 90, No. 3 (1993), p. 1132-1136
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Format: Online-Artikel
Sprache: English
Veröffentlicht: 1993
Beschreibung: Online-Ressource
Schlagworte: research-article
Plant Biology
Iron-Sulfur Center Fx
Leucine Zipper
Photosynthesis
psaB Gene
Site-Directed Mutagenesis
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Anmerkung: Copyright: Copyright 1993 The National Academy of Sciences of the United States of America
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520 |a We have utilized the unicellular cyanobacterium Synechocystis sp. PCC 6803 to incorporate site-directed amino acid substitutions into the photosystem I (PSI) reactioncenter protein PsaB. A cysteine residue (position 565 of PsaB) proposed to serve as a ligand to the [4Fe-4S] center Fxwas changed to serine, histidine, and aspartate. These three mutants-C565S, C565H, and C565D-all exhibited greatly reduced accumulation of PSI reaction-center proteins and failed to grow autotrophically, indicating that this cysteine most likely does coordinate Fx, which is crucial for PSI biogenesis. Interestingly, the strain C565S accumulated significantly more PSI than the other two cysteine mutants and displayed photoreduction of the [4Fe-4S] terminal electron acceptors FAand FB. Mutations were also introduced into a leucine zipper motif of PsaB, proposed to participate in reaction-center dimerization. The mutants L522V, L536M, and L522V/L536M all exhibited wild-type characteristics and grew autotrophically, whereas the L522P mutation prevented PSI accumulation. These data do not provide support for a major structural role of the leucine zipper in reaction-center dimerization or in assembly of Fx. However, the amino acid substitutions incorporated were conservative and might not have perturbed the leucine zipper. 
653 |a research-article 
653 |a Plant Biology 
653 |a Iron-Sulfur Center Fx 
653 |a Leucine Zipper 
653 |a Photosynthesis 
653 |a psaB Gene 
653 |a Site-Directed Mutagenesis 
773 0 8 |i in  |t Proceedings of the National Academy of Sciences of the United States of America  |d Washington, DC : National Acad. of Sciences  |g Vol. 90, No. 3 (1993), p. 1132-1136  |q 90:3<1132-1136  |w (DE-601)JST069399220  |x 0027-8424 
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