Plant Physiology Preview
Published on May 5, 2006; 10.1104/pp.106.078147
Received January 30, 2006
Returned for revision February 27, 2006
Accepted March 27, 2006
The evolutionary conserved TPR protein Pyg7 is required for photosystem I accumulation in Arabidopsis thaliana and co-purifies with the complex
Jana Stöckel , Stefan Bennewitz , Paul Hein , and Ralf Oelmüller *
Institut für Allgemeine Botanik und Pflanzenphysiologie, Friedrich-Schiller-Universität Jena, Dornburger Str. 159, 07747 Jena, Germany
* Corresponding author; email: b7oera{at}hotmail.com.
Pyg7-1 (pale yellow green) is a photosystem I-deficient Arabidopsis mutant. Photosystem I subunits are synthesized in the mutant but do not assemble into a stable complex. In contrast, light-harvesting antenna proteins of both photosystems accumulate in the mutant. Deletion of Pyg7 results in severely reduced growth rates, alterations in leaf coloration and plastid ultrastructure. Pyg7 was isolated by map-based cloning and encodes a TPR protein with homology to Ycf37 from Synechocystis (Wilde et al., 2001). The protein is localized in the chloroplast, associated with thylakoid membranes and co-purifies with photosystem I. An independent pyg7 T-DNA insertion line pyg7-2 exhibits the same phenotype. pyg7 gene expression is light-regulated. Comparison of the roles of Ycf37 in cyanobacteria and Pyg7 in higher plants suggests that the ancient protein has altered it function during the evolution. While the cyanobacterial protein mediates more efficient photosystem I accumulation, the higher plant protein is absolutely required for complex assembly or maintenance.
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