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Originally published In Press as doi:10.1074/jbc.M011525200 on February 2, 2001

J. Biol. Chem., Vol. 276, Issue 18, 15275-15283, May 4, 2001
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Overlapping Destinations for Two Dual Targeted Glycyl-tRNA Synthetases in Arabidopsis thaliana and Phaseolus vulgaris*

Anne-Marie DuchêneDagger §, Nemo Peeters, André DietrichDagger , Anne CossetDagger , Ian D. Small, and Henri WintzDagger ||

From the Dagger  Institut de Biologie Moléculaire des Plantes du CNRS, Université, CNRS Université Louis Pasteur, 12 Rue du Général Zimmer, F-67084 Strasbourg Cedex, France and the  Station de Génétique et d'Amélioration des Plantes, Institut National de la Recherche Agronomique, Route de St.-Cyr, F-78026 Versailles Cedex, France

In plant mitochondria, some of the tRNAs are encoded by the mitochondrial genome and resemble their prokaryotic counterparts, whereas the remaining tRNAs are encoded by the nuclear genome and imported from the cytosol. Generally, mitochondrial isoacceptor tRNAs all have the same genetic origin. One known exception to this rule is the group of tRNAGly isoacceptors in dicotyledonous plants. A mitochondrion-encoded tRNAGly and at least one nucleus-encoded tRNAGly coexist in the mitochondria of these plants, and both are required to allow translation of all four GGN glycine codons. We have taken advantage of this atypical situation to address the problem of tRNA/aminoacyl-tRNA synthetase coevolution in plants. In this work, we show that two different nucleus-encoded glycyl-tRNA synthetases (GlyRSs) are imported into Arabidopsis thaliana and Phaseolus vulgaris mitochondria. The first one, GlyRS-1, is similar to human or yeast glycyl-tRNA synthetase, whereas the second, GlyRS-2, is similar to Escherichia coli glycyl-tRNA synthetase. Both enzymes are dual targeted, GlyRS-1 to mitochondria and to the cytosol and GlyRS-2 to mitochondria and chloroplasts. Unexpectedly, GlyRS-1 seems to be active in the cytosol but inactive in mitochondrial fractions, whereas GlyRS-2 is likely to glycylate both the organelle-encoded tRNAGly and the imported tRNAGly present in mitochondria.


* This work was supported by the CNRS, the Université Louis Pasteur (Strasbourg), and the Institut National de la Recherche Agronomique and by a grant from the Groupement de Recherche et d'Etude des Génomes.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed. Fax: 33 3 88 61 44 42; E-mail: anne-marie.duchene@ibmp-ulp.u-strasbg.fr.

|| Current address: Nutrition and Toxicology, 119 Koshland Hall, University of California, Berkeley, CA 94720.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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