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Originally published In Press as doi:10.1074/jbc.M100727200 on March 2, 2001

J. Biol. Chem., Vol. 276, Issue 22, 19363-19374, June 1, 2001
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The Small Subunit of the Mammalian Mitochondrial Ribosome
IDENTIFICATION OF THE FULL COMPLEMENT OF RIBOSOMAL PROTEINS PRESENT*

Emine Cavdar KocDagger , William Burkhart§, Kevin Blackburn§, Arthur Moseley§, and Linda L. SpremulliDagger

From the Dagger  Department of Chemistry and Campus Box 3290, University of North Carolina, Chapel Hill, North Carolin 27599-3290 and § GlaxoSmithKline Research and Development, Department of Structural Chemistry, Research Triangle, North Carolina 27709-3398

Identification of all the protein components of the small subunit (28 S) of the mammalian mitochondrial ribosome has been achieved by carrying out proteolytic digestions of whole 28 S subunits followed by analysis of the resultant peptides by liquid chromatography and tandem mass spectrometry (LC/MS/MS). Peptide sequence information was used to search the human EST data bases and complete coding sequences of the proteins were assembled. The human mitochondrial ribosome has 29 distinct proteins in the small subunit. Fourteen of this group of proteins are homologs of the Escherichia coli 30 S ribosomal proteins S2, S5, S6, S7, S9, S10, S11, S12, S14, S15, S16, S17, S18, and S21. All of these proteins have homologs in Drosophila melanogaster, Caenorhabditis elegans, and Saccharomyces cerevisiae mitochondrial ribosomes. Surprisingly, three variants of ribosomal protein S18 are found in the mammalian and D. melanogaster mitochondrial ribosomes while C. elegans has two S18 homologs. The S18 homologs tend to be more closely related to chloroplast S18s than to prokaryotic S18s. No mitochondrial homologs to prokaryotic ribosomal proteins S1, S3, S4, S8, S13, S19, and S20 could be found in the peptides obtained from the whole 28 S subunit digests or by analysis of the available data bases. The remaining 15 proteins present in mammalian mitochondrial 28 S subunits (MRP-S22 through MRP-S36) are specific to mitochondrial ribosomes. Proteins in this group have no apparent homologs in bacterial, chloroplast, archaebacterial, or cytosolic ribosomes. All but two of these proteins have a clear homolog in D. melanogaster while all but three can be found in the genome of C. elegans. Five of the mitochondrial specific ribosomal proteins have homologs in S. cerevisiae.

* This work has been supported by National Institutes of Health Grant GM32734.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. Tel.: 919-966-1567; Fax: 919-966-3675; E-mail: Linda_Spremulli@unc.edu.

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