Plant Physiology Preview
Published on June 15, 2007; 10.1104/pp.107.103218
OPEN ACCESS ARTICLE
Received June 1, 2007
Accepted June 11, 2007
A Novel Nucleus-encoded Chloroplast Protein, PIFI, Is Involved in NAD(P)H Dehydrogenase Complex Mediated Chlororespiratory Electron Transport in Arabidopsis
Dafu Wang and Archie R Portis Jr. *
Department of Plant Biology, University of Illinois, 190 E. R. Madigan Laboratory, 1201 W Gregory Dr., Urbana IL 61801, USA; U.S. Department of Agriculture, Photosynthesis Research Unit, Agricultural Research Service, 1201 W Gregory Dr., Urbana IL 61801, USA
* Corresponding author; email: arportis{at}uiuc.edu.
A transient rise in chlorophyll fluorescence after turning off actinic light reflects non-photochemical reduction of the plastoquinone pool. This process is dependent on the activity of the chloroplast NAD(P)H-dehydrogease complex (NDH) which mediates electron flow from stromal reductants to the plastoquinone pool. In this study, we characterized an Arabidopsis thaliana T-DNA insertion mutant pifi (post-illumination chlorophyll fluorescence increase), which possesses an intact NDH complex but lacks the NDH-dependent chlorophyll fluorescence increase after turning off actinic light. The nuclear gene PIFI (At3g15840) containing the T-DNA insertion encodes a chloroplast-targeted protein localized in the stroma and is annotated as a protein of unknown function. The pifi mutant exhibited a lower capacity for thermal dissipation (NPQ) but similar CO2 assimilation rates, PSII quantum efficiencies ( PSII) and reduction levels of the primary electron acceptor of PSII (1-qL) as compared with the wild type. The pifi mutant grows normally under optimal conditions but exhibits a greater sensitivity to photoinhibition and long-term mild heat stress than wild type plants, which is consistent with lower capacity of NPQ. We conclude that PIFI is a novel component essential for NDH-mediated non-photochemical reduction of the plastoquinone pool in chlororespiratory electron transport.
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