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Originally published In Press as doi:10.1074/jbc.M010864200 on February 14, 2001

J. Biol. Chem., Vol. 276, Issue 19, 15861-15867, May 11, 2001
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Identification of 12 New Yeast Mitochondrial Ribosomal Proteins Including 6 That Have No Prokaryotic Homologues*

Cosmin SaveanuDagger §, Micheline Fromont-RacineDagger , Alexis Harington||, Florence RicardDagger , Abdelkader Namane**, and Alain JacquierDagger Dagger Dagger

From the Dagger  Génétique des Interactions Macromoléculaires, CNRS (URA2171),  Génétique Moléculaire des Levures, CNRS (URA2171), and ** Chimie Structurale des Macromolécules, CNRS (URA2185), Institut Pasteur, 25-28 Rue du Dr. Roux, 75724 Paris Cedex 15, France

Mitochondrial ribosomal proteins were studied best in yeast, where the small subunit was shown to contain about 35 proteins. Yet, genetic and biochemical studies identified only 14 proteins, half of which were predictable by sequence homology with prokaryotic ribosomal components of the small subunit. Using a recently described affinity purification technique and tagged versions of yeast Ykl155c and Mrp1, we isolated this mitochondrial ribosomal subunit and identified a total of 20 proteins, of which 12 are new. For a subset of the newly described ribosomal proteins, we showed that they are localized in mitochondria and are required for the respiratory competency of the yeast cells. This brings to 26 the total number of proteins described as components of the mitochondrial small ribosomal subunit. Remarkably, almost half of the previously and newly identified mitochondrial ribosomal components showed no similarity to any known ribosomal protein. Homologues could be found, however, in predicted protein sequences from Schizosaccharomyces pombe. In more distant species, putative homologues were detected for Ykl155c, which shares conserved motifs with uncharacterized proteins of higher eukaryotes including humans. Another newly identified ribosomal protein, Ygl129c, was previously shown to be a member of the DAP-3 family of mitochondrial apoptosis mediators.

* This work was supported by grants from Groupe d'Interet Publique-Aventis, CNRS, and Ministere de l'Education Nationale (France).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.

§ Recipient of financial support from Groupe d'Interet Publique- Aventis.

|| Supported by a grant (EUROFAN2 Bio4-CT97-2294) from the European Economic Community.

Dagger Dagger To whom correspondence should be addressed. Tel.: 33 140 613 205; Fax: 33 145 688 790; E-mail: jacquier@pasteur.fr.

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