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Publication : A proteomics approach to the identification of mammalian mitochondrial small subunit ribosomal proteins.

First Author  Koc EC Year  2000
Journal  J Biol Chem Volume  275
Issue  42 Pages  32585-91
PubMed ID  10938081 Mgi Jnum  J:65190
Mgi Id  MGI:1913180 Doi  10.1074/jbc.M003596200
Citation  Koc EC, et al. (2000) A proteomics approach to the identification of mammalian mitochondrial small subunit ribosomal proteins. J Biol Chem 275(42):32585-91
abstractText  Mammalian mitochondrial small subunit ribosomal proteins were separated by two-dimensional polyacrylamide gel electrophoresis. The proteins in six individual spots were subjected to in-gel tryptic digestion. Peptides were separated by capillary liquid chromatography, and the sequences of selected peptides were obtained by electrospray tandem mass spectrometry. The peptide sequences obtained were used to screen human expressed sequence tag data bases, and complete consensus cDNAs were assembled. Mammalian mitochondrial small subunit ribosomal proteins from six different classes of ribosomal proteins were identified. Only two of these proteins have significant sequence similarities to ribosomal proteins from prokaryotes. These proteins correspond to Escherichia coli S10 and S14. Homologs of two human mitochondrial proteins not found in prokaryotes were observed in the genomes of Drosophila melanogaster and Caenorhabditis elegans. A homolog of one of these proteins was observed in D. melanogaster but not in C. elegans, while a homolog of the other was present in C. elegans but not in D. melanogaster. A homolog of one of the ribosomal proteins not found in prokaryotes was tentatively identified in the yeast genome. This latter protein is the first reported example of a ribosomal protein that is shared by mitochondrial ribosomes from lower and higher eukaryotes that does not have a homolog in prokaryotes.
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