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Plant Cell Advance Online Publication
Published on October 26, 2007; 10.1105/tpc.107.054841

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Received August 7, 2007
Returned for revision September 26, 2007
Accepted October 3, 2007

The Pentatricopeptide Repeat Gene OTP43 Is Required for trans-Splicing of the Mitochondrial nad1 Intron 1 in Arabidopsis thaliana

Andéol Falcon de Longevialle 1, Etienne H. Meyer 2, Charles Andrés 3, Nicolas L. Taylor 2, Claire Lurin 3, A. Harvey Millar 2, and Ian D. Small 1*

1 Unité Mixte de Recherche Génomique Végétale (Institut National de la Recherche Agronomique, Centre National de la Recherche Scientifique, Université d'Evry/Val d'Essonne), 91057 Evry, France; Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley 6009 WA, Australia
2 Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley 6009 WA, Australia
3 Unité Mixte de Recherche Génomique Végétale (Institut National de la Recherche Agronomique, Centre National de la Recherche Scientifique, Université d'Evry/Val d'Essonne), 91057 Evry, France

* To whom correspondence should be addressed. E-mail: iansmall{at}cyllene.uwa.edu.au.

The mitochondrial NADH:ubiquinone oxidoreductase complex (Complex I) is a large protein complex formed from both nuclearly and mitochondrially encoded subunits. Subunit ND1 is encoded by a mitochondrial gene comprising five exons, and the mature transcript requires four RNA splicing events, two of which involve trans-splicing independently transcribed RNAs. We have identified a nuclear gene (OTP43) absolutely required for trans-splicing of intron 1 (and only intron 1) of Arabidopsis thaliana nad1 transcripts. This gene encodes a previously uncharacterized pentatricopeptide repeat protein. Mutant Arabidopsis plants with a disrupted OTP43 gene do not present detectable mitochondrial Complex I activity and show severe defects in seed development, germination, and to a lesser extent in plant growth. The alternative respiratory pathway involving alternative oxidase is significantly induced in the mutant.




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