《Recruitment of a Ribosomal Release Factor for Light- and》.pdf

The Plant Cell, Vol. 23: 2680–2695, July 2011, ã 2011 American Society of Plant Biologists. All rights reserved. Recruitment of a Ribosomal Release Factor for Light- and Stress-Dependent Regulation of petB Transcript Stability in Arabidopsis Chloroplasts W OA Rhea Stoppel,a Lina Lezhneva,a,1 Serena Schwenkert,a Salar Torabi,a Susanne Felder,b Karin Meierhoff,b b ¨ a,2 Peter Westhoff, and Jorg Meurer a ¨ Biozentrum der Ludwig-Maximilians-Universitat, Plant Molecular Biology/Botany, 82 152 Planegg-Martinsried, Germany b ¨ ¨ Heinrich-Heine-Universitat, Institut fur Entwicklungs- und Molekularbiologie der Pflanzen, 40225 Duesseldorf, Germany Land plant genomes encode four functional ribosomal peptide chain release factors (Prf) of eubacterial origin, two (PrfA and PrfB homologs) for each endosymbiotic organelle. Formerly, we have shown that the Arabidopsis thaliana chloroplast- localized PrfB homolog, PrfB1, is required not only for termination of translation but also for stabilization of UGA stop codon-containing chloroplast transcripts. A previously undiscovered PrfB-like protein, PrfB3, is localized to the chloroplast stroma in a petB RNA-containing complex and found only in vascular plants. Highly conserved positions of introns unequivocally indicate that PrfB3 arose from a duplication of PrfB1. Notably, PrfB3 is lacking the two most important tripeptide motifs characteristic for all eubacterial and organellar PrfB homologs described so far: the stop codon recognition motif SPF and the catalytic center GGQ for peptidyl-tRNA hydrolysis. Complement