Plants respond to changing light conditions by altering the stoichiometry between components of the photosynthetic electron transport chain of chloroplast thylakoids. We measured specific run-on transcription of the chloroplast genes psaB, psbA and rbcL in pea (Pisum sativum L.) seedlings grown under three different conditions of illumination: light selective for photosystem I (PSI-light); light selective for photosystem II (PSII-light); and a combination of PSI- and PSII-light (mixed light, ML). The transcriptional rate of the psaB gene increased under PSII-light and decreased under PSI-light, while the transcriptional rates of the psbA and rbcL genes were affected only in a non-specific way. Similar effects also occurred in plants grown under ML and switched to either PSI- or PSII-light for 4 h. Addition of the inhibitors of photosynthetic electron transport 3-(3,4 dichlorophenyl)-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB) influenced psaB transcription in isolated, illuminated chloroplasts: DCMU addition resulted in oxidation of the plastoquinone pool and decreased transcription of psaB; DBMIB addition resulted in reduction of the plastoquinone pool and increased transcription of psaB. The experimental results obtained in vivo and in vitro provide evidence for coupling between the redox state of plastoquinone and the rate of transcription of the psaB gene in pea.
Photosynthesis is light-driven redox chemistry. Molecular redox signalling, the coupling of gene expression to electron transfer, is now implicated in the adaptation of photosynthesis to variation in light quality and quantity.
Two protease activities of pea chloroplasts, one located in the stroma and the other associated to the thylakoid membrane, are described. Both proteases catalyse the endo-proteolytic cleavage of a peptide corresponding to the N-terminal loop and the first turn in helix-B of light-harvesting complex II (Lhcb1 from pea). The stromal protease cleaves preferentially on the carboxy-side of glutamic acid residues. Inhibitor studies indicate that this protease is a serine-type protease. The protease was partially purified and could be correlated to a 95-kDa polypeptide band on SDS-polyacrylamide gels. The 95 kDa protein was partially sequenced and showed similarity to an to an 'unknown protein' from A. thaliana (in the NCBI public database) as well as to a glutamyl endopeptidase purified from crude extract of cucumber leaves. It is concluded that the stromal protease is a chloroplast glutamyl endopeptidase (cGEP). The protease localized in the thylakoid membrane, cleaved the peptide at only one site, close to its N terminus. The activity of the thylakoid-associated protease was found to be drastically increased in the presence of the reducing agent 1,4-dithiothreitol. Inhibitor studies suggest that this protease is a cysteine-or serine-type protease. The possible roles of these proteases in the regulation of photosynthetic electron transport and in the chloroplast homeostasis are discussed.
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