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J Biol Chem, Vol. 274, Issue 51, 36043-36051, December 17, 1999

Mammalian Mitochondrial Ribosomal Proteins (2)
AMINO ACID SEQUENCING, CHARACTERIZATION, AND IDENTIFICATION OF CORRESPONDING GENE SEQUENCES*

Thomas W. O'BrienDagger , Scott E. FieslerDagger , Nancy D. DenslowDagger , Bernd Thiede§, Brigitte Wittmann-Liebold§, Edward B. Mougey, James E. Sylvester, and Hanns-Rüdiger Graack||**

From the Dagger  Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, Florida 32610-0245, § Max-Delbrück-Center for Molecular Medicine, Robert-Rössle-Str. 10, D-13125 Berlin, Germany,  Nemours Children's Clinic, Research, Jacksonville, Florida 32207, and the || Institute for Biology-Genetics, AG Kress, Free University of Berlin, Arnimallee 7, D-14195 Berlin, Germany

Four different classes of mammalian mitochondrial ribosomal proteins were identified and characterized. Mature proteins were purified from bovine liver and subjected to N-terminal or matrix-assisted laser-desorption mass spectroscopic amino acid sequencing after tryptic in-gel digestion and high pressure liquid chromatography separation of the resulting peptides. Peptide sequences obtained were used to virtually screen expressed sequence tag data bases from human, mouse, and rat. Consensus cDNAs were assembled in silico from various expressed sequence tag sequences identified. Deduced mammalian protein sequences were characterized and compared with ribosomal protein sequences of Escherichia coli and yeast mitochondria. Significant sequence similarities to ribosomal proteins of other sources were detected for three out of four different mammalian protein classes determined. However, the sequence conservation between mitochondrial ribosomal proteins of mammalian and yeast origin is much less than the sequence conservation between cytoplasmic ribosomal proteins of the same species. In particular, this is shown for the mammalian counterparts of the E. coli EcoL2 ribosomal protein (MRP-L14), that do not conserve the specific and functional highly important His229 residue of E. coli and the corresponding yeast mitochondrial Rml2p.

* This work was supported by United States Public Health Service Grant GM15438 (to T. W. O.).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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) S78756 (MRP-L5bov), S78757 (MRP-L7bov), S78758 (MRP-L14bov), and S78759 (MRP-L26bov), respectively.

** To whom correspondence should be addressed: Inst. for Biology-Genetics, AG Kress, Free University of Berlin, Arnimallee 7, D-14195 Berlin, Germany. Tel.: 49-30-838-2629; Fax: 49-30-838-3649; E-mail: graack@zedat.fu-berlin.de.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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