A novel mechanism of nuclear photosynthesis gene regulation by redox signals from the chloroplast during photosystem stoichiometry adjustment.
Photosynthetic organisms acclimate to long term changes in the environmental light quality by an adjustment of their photosystem stoichiometry to maintain photosynthetic efficiency. By using light sources that predominantly excite either photosystem I (PSI) or photosystem II (PSII), we studied the effects of excitation imbalances between both photosystems on nuclear PSI gene transcription in transgenic tobacco seedlings with promoter::beta-glucuronidase gene fusions. Shifts from PSI to PSII light sources (and vice versa) induced changes in the reduction/oxidation state of intersystem redox components, and acclimation of tobacco seedlings to such changes were monitored by changes in chlorophyll a/b ratios and in vivo chlorophyll a fluorescence. The ferredoxin-NADP(+)-oxidoreductase gene promoter did not respond to these treatments, those from the genes for subunits PsaD and PsaF of PSI are activated by a reduction signal, and the plastocyanin promoter responded to both reduction and oxidation signals. Additional experiments with photosynthetic electron transport inhibitors 3-(3',4'-dichlorophenyl)-1,1'-dimethyl urea and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone demonstrated that the redox state of the plastoquinone pool controls the activity of the plastocyanin promoter, whereas subunit PsaD and PsaF gene transcription is regulated by other photosynthesis-derived signals. Thus, the expression of nuclear-encoded PSI genes is controlled by diverse light quality-dependent redox signals from the plastids during photosystem stoichiometry adjustment.
Pfannschmidt
T
T
Institute of General Botany, Department of Plant Physiology, University of Jena, Dornburger Strasse 159, 07743 Jena, Germany. Thomas.Pfannschmidt@uni-jena.de
Schütze
K
K
Brost
M
M
Oelmüller
R
R
D001665:Binding Sites; D002467:Cell Nucleus / Q000378:metabolism*; D002736:Chloroplasts / Q000378:metabolism*; D003991:Dibromothymoquinone / Q000494:pharmacology; D004237:Diuron / Q000494:pharmacology; D004579:Electron Transport; D005287:Ferredoxin-NADP Reductase / Q000235:genetics; D006540:Herbicides / Q000494:pharmacology; D008027:Light; D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins / Q000235:genetics; D009149:Mustard Plant / Q000201:enzymology / Q000235:genetics; D010084:Oxidation-Reduction; D010788:Photosynthesis / Q000235:genetics*; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D045332:Photosystem II Protein Complex; D010940:Plant Proteins / Q000235:genetics; D010946:Plants, Medicinal; D010947:Plants, Toxic; D010970:Plastocyanin / Q000235:genetics; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013050:Spectrometry, Fluorescence; D013997:Time Factors; D014026:Nicotiana / Q000201:enzymology / Q000235:genetics; D014158:Transcription, Genetic
D006540:Herbicides; D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; C070290:PsaD protein, cyanobacteria; D003991:Dibromothymoquinone; D010970:Plastocyanin; D004237:Diuron; D005287:Ferredoxin-NADP Reductase