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Plant Physiology 127 (3): 1044-1052

Copyright © 2001 by the American Society of Plant Physiologists.

Plant Physiol, November 2001, Vol. 127, pp. 1044-1052

Chloroplast Transcription at Different Light Intensities. Glutathione-Mediated Phosphorylation of the Major RNA Polymerase Involved in Redox-Regulated Organellar Gene Expression1

Elena Baena-González,2 Sacha Baginsky,23 Paula Mulo, Holger Summer, Eva-Mari Aro, and Gerhard Link*

Department of Biology, University of Turku, FIN-20014 Turku, Finland (E.B.-G., P.M., E.-M.A.); and Plant Cell Physiology, University of Bochum, D-44780 Bochum, Germany (S.B., H.S., G.L.)

Previous studies using purified RNA polymerase from mustard (Sinapis alba) chloroplasts showed control of transcription by an associated protein kinase. This kinase was found to respond to reversible thiol/disulfide formation mediated by glutathione (GSH), although at concentrations exceeding those thought to exist in vivo. In the present study, several lines of evidence are presented to substantiate the functioning of this regulation mechanism, also in vivo: (a) Studies on the polymerase-associated transcription kinase revealed that at appropriate ATP levels, GSH concentrations similar to those in vivo are sufficient to modulate the kinase activity; (b) GSH measurements from isolated mustard chloroplasts showed considerable differences in response to light intensity; (c) this was reflected by run-on transcription rates in isolated chloroplasts that were generally higher if organelles were prepared from seedlings incubated under high-light as compared with growth-light conditions; (d) the notion of a general transcriptional switch was strengthened by in vitro experiments showing that the kinase not only affects the transcription of a photosynthetic gene (psbA) but also that of a non-photosynthetic gene (trnQ); and (e) the polymerase-kinase complex revealed specific differences in the phosphorylation state of polypeptides depending on the light intensity to which the seedlings had been exposed prior to chloroplast isolation. Taken together, these data are consistent with GSH and phosphorylation-dependent regulation of chloroplast transcription in vivo.

1 This work was supported by the Academy of Finland (grant to E.-M.A.), by the Deutsche Akademische Austausdienst, by the Deutsche Forschungsgemeinschaft, and by the Fonds der Chemischen Industrie (to G.L.).

2 These authors contributed equally to the paper.

3 Present address: Plant Science Institute, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092 Zürich, Switzerland.

* Corresponding author; e-mail Gerhard.Link{at}; fax 49-234-3214-188.

© 2001 American Society of Plant Physiologists

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