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J. Biol. Chem., Vol. 276, Issue 49, 45642-45653, December 7, 2001
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From the In vivo, human mitochondria
import 5 S rRNA and do not import tRNAs from the cytoplasm. We
demonstrated previously that isolated human mitochondria are able to
internalize a yeast tRNALys in the presence of yeast
soluble factors. Here, we describe an assay for specific uptake of 5 S
rRNA by isolated human mitochondria and compare its requirements with
the artificial tRNA import. The efficiency of 5 S rRNA uptake by
isolated mitochondria was comparable with that found in
vivo. The import was shown to depend on ATP and the transmembrane
electrochemical potential and was directed by soluble proteins.
Blocking the pre-protein import channel inhibited internalization of
both 5 S rRNA and tRNA, which suggests this apparatus be involved in
RNA uptake by the mitochondria. We show that human mitochondria can
also selectively internalize several in vitro synthesized
versions of yeast tRNALys as well as a transcript of the
human mitochondrial tRNALys. Either yeast or human soluble
proteins can direct this import, suggesting that human cells possess
all factors needed for such an artificial translocation. On the other
hand, the efficiency of import directed by yeast or human protein
factors varies significantly, depending on the tRNA version. Similarly
to the yeast system, tRNALys import into human mitochondria
depended on aminoacylation and on the precursor of the mitochondrial
lysyl-tRNA synthetase. 5 S rRNA import was also dependent upon soluble
protein(s), which were distinct from the factors providing tRNA internalization.
5 S rRNA and tRNA Import into Human Mitochondria
COMPARISON OF IN VITRO
REQUIREMENTS*
§¶,§
,,, and**
Formation de Recherche en Evolution 2375, CNRS "Modèles d'Etude de Pathologies Humaines," 21 rue
René Descartes, 67084 Strasbourg, France and the
§ Department of Molecular Biology, Biology Faculty,
Moscow State University, 119899 Moscow, Russia
*
This work was supported in part by CNRS, Université
Louis Pasteur, Moscow State University, Association Française
contre les Myopathies (AFM), International Association for Promotion of
Cooperation with Scientists from the New Independent States of the
Former Soviet Union (INTAS) Grant 96-1515, (Human Frontier Science
Program (HSFP) Grant RG0349/1999-M, and Russian Foundation for Basic
Research Grant 00-04-48488.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.
Supported by INTAS, Federation of European Biochemical
Societies (FEBS), and AFM.
**
To whom correspondence should be addressed. Tel.: 33-3-90-24-14-60;
Fax: 33-3-88-41-70-70; E-mail:
i.tarassov@ibmc.u-strasbg.fr.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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