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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
Overlapping Destinations for Two Dual Targeted Glycyl-tRNA
Synthetases in Arabidopsis thaliana and Phaseolus
vulgaris*
Anne-Marie
Duchêne §,
Nemo
Peeters¶,
André
Dietrich ,
Anne
Cosset ,
Ian D.
Small¶, and
Henri
Wintz
From the 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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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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