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Plant and Cell Physiology Advance Access originally published online on June 9, 2005
Plant and Cell Physiology 2005 46(8):1433-1436; doi:10.1093/pcp/pci147
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JSPP © 2005

Short Communication

Open Reading Frame ssr2016 is Required for Antimycin A-sensitive Photosystem I-driven Cyclic Electron Flow in the Cyanobacterium Synechocystis sp. PCC 6803

Nataliya Yeremenko1, Robert Jeanjean2, Peerada Prommeenate3, Vladimir Krasikov1, Peter J. Nixon3, Wim F. J. Vermaas4, Michel Havaux5 and Hans C. P. Matthijs1,*

1 Aquatic Microbiology, Institute for Biodiversity and Ecosystem Dynamics, Faculty of Science, University of Amsterdam, Nieuwe Achtergracht 127, 1018 WS Amsterdam, The Netherlands
2 LCB-CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France
3 Wolfson Biochemistry Building, Department of Biological Sciences, Imperial College, London, South Kensington Campus, London SW7 2AZ, UK
4 School of Life Sciences and Photosynthesis Center, Arizona State University, PO Box 874501, Tempe, AZ 85287-4501, USA
5 CEA/Cadarache, DSV, DEVM, Laboratoire d’Ecophysiologie de la Photosynthèse, UMR 6191 CNRS-CEA-Aix Marseille II, 13108 Saint-Paul-lez-Durance, France

* Corresponding author: Email, hansmatt{at}science.uva.nl; Fax, +31-205257064.

Open reading frame ssr2016 encodes a protein with substantial sequence similarities to PGR5 identified as a component of the antimycin A-sensitive ferredoxin:plastoquinone reductase (FQR) in PSI cyclic photophosphorylation in Arabidopsis thaliana. We studied cyclic electron flow in Synechocystis sp. PCC 6803 in vivo in ssr2016 deletion mutants generated either in a wild-type background or in a ndhB deletion mutant. Our results indicate that ssr2016 is required for FQR and that it operates in a parallel pathway to the NDH1 complex. The ssr2016 deletion mutants are high light sensitive, suggesting that FQR might be important in controlling redox poise under adverse conditions.

(Received December 27, 2004; Accepted June 2, 2005)
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