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Identification of four proteins from the small subunit of the mammalian mitochondrial ribosome using a proteomics approach

¹ Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA
² Glaxo Wellcome Research and Development Department of Analytical Chemistry, Research Triangle Park, North Carolina 27709, USA
³ School of Public Health, Environmental Sciences and Engineering, University of North Carolina, Chapel Hill, North Carolina 27599–3290, USA

Reprint request to: Linda L. Spremulli, Department of Chemistry, Campus Box 3290, University of North Carolina, North Carolina 27599-3290, USA; e-mail: Linda_Spremulli{at}unc.edu; fax: (999) 966–3675.

Proteins in the small subunit of the mammalian mitochondrial ribosome were separated by two-dimensional polyacrylamide gel electrophoresis. Four individual proteins were subjected to in-gel Endoprotease Lys-C digestion. The sequences of selected proteolytic peptides were obtained by electrospray tandem mass spectrometry. Peptide sequences obtained from in-gel digestion of individual spots were used to screen human, mouse, and rat expressed sequence tag databases, and complete consensus cDNAs for these species were deduced in silico. The corresponding protein sequences were characterized by comparison to known ribosomal proteins in protein databases. Four different classes of mammalian mitochondrial small subunit ribosomal proteins were identified. Only two of these proteins have significant sequence similarities to ribosomal proteins from prokaryotes. These proteins are homologs to Escherichia coli S9 and S5 proteins. The presence of these newly identified mitochondrial ribosomal proteins are also investigated in the Drosophila melanogaster, Caenorhabditis elegans, and in the genomes of several fungi.

Keywords: Mitochondria; protein synthesis; ribosome; proteomics; mass spectrometry; ribosomal protein

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