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BIOLOGICAL SCIENCES / PLANT BIOLOGY
Three thioredoxin targets in the inner envelope membrane of chloroplasts function in protein import and chlorophyll metabolism

Sandra Bartsch^*, Julie Monnet, Kristina Selbach, Françoise Quigley, John Gray, Diter von Wettstein^,¶, Steffen Reinbothe, and Christiane Reinbothe^*,,¶

*Lehrstuhl für Pflanzenphysiologie, Universität Bayreuth, Universitätsstrasse 30, D-95447 Bayreuth, Germany; Unité Mixte de Recherche 5575, Centre d'Etudes et de Recherches sur les Macromolécules Organiques, Université Joseph Fourier et Centre National de la Recherche Scientifique, BP53, F-38041 Grenoble Cedex 9, France; Department of Biological Sciences, University of Toledo, 2801 West Bancroft Street, Toledo, OH 43606; and Department of Crop and Soil Sciences and School of Molecular Biosciences, Washington State University, Pullman WA 99164-6420

Contributed by Diter von Wettstein, January 16, 2008 (received for review December 11, 2007)

Thioredoxins (Trxs) are ubiquitous small proteins with a redox-active disulfide bridge. In their reduced form, they constitute very efficient protein disulfide oxidoreductases. In chloroplasts, two types of Trxs (f and m) coexist and play central roles in the regulation of the Calvin cycle and other processes. Here, we identified a class of Trx targets in the inner plastid envelope membrane of chloroplasts that share a CxxC motif 73 aa from their carboxyl-terminal end. Members of this group belong to a superfamily of Rieske iron–sulfur proteins involved in protein translocation and chlorophyll metabolism. These proteins include the protein translocon protein TIC55, the precursor NADPH:protochlorophyllide oxidoreductase translocon protein PTC52, which operates as protochlorophyllide a-oxygenase, and the lethal leaf spot protein LLS1, which is identical with pheophorbide a oxygenase. The role of these proteins in dark/light regulation and oxidative control by the Trx system is discussed.

protein translocation | tetrapyrrole biosynthesis | Tigrina d12 | FLU mutant | photooxidative stress

The authors declare no conflict of interest.

This article contains supporting information online at www.pnas.org/cgi/content/full/0800378105/DC1.

^¶To whom correspondence may be addressed. E-mail: diter{at}wsu.edu or christiane.reinbothe{at}uni-bayreuth.de

© 2008 by The National Academy of Sciences of the USA

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