Mammalian mitochondrial ribosomal proteins (4) - Amino acid sequencing, characterization, and identification of corresponding gene sequences

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Item Type:	Article
Title:	Mammalian mitochondrial ribosomal proteins (4) - Amino acid sequencing, characterization, and identification of corresponding gene sequences
Creators Name:	O'Brien, T.W., Liu, J.G., Sylvester, J.E., Mougey, E.B., Fischel-Ghodsian, N., Thiede, B., Wittmann-Liebold, B. and Graack, H.R.
Abstract:	Mitochondrial ribosomal proteins (MRPs) are required for the translation of all 13 mitochondrial encoded genes in humans. It has been speculated that mutations and polymorphisms in the human MRPs may be a primary cause of some oxidative phosphorylation disorders or modulate the severity and tissue specificity of pathogenic mitochondrial DNA mutations. Although the sequences of most of the yeast MRPs are known, only very few mammalian and nearly no human MRPs have been completely characterized. MRPs differ greatly in sequence, and sometimes biochemical properties, between different species, not allowing easy recognition by sequence homology. Therefore, the Mammalian Mitochondrial Ribosomal Consortium is using a direct approach of purifying individual mammalian (bovine) MRPs, determining their N-terminal and/or internal peptide sequences using different protein sequencing techniques, and using the resulting sequence information for screening expressed sequence tags and genomic data bases to determine human, mouse, and rat homologues of the bovine proteins. Two proteins of the large and three proteins of the small ribosomal subunit have been analyzed in this manner. Three of them represent 'new,' i.e. formerly unknown mammalian mitochondrial ribosomal protein classes. Only one of these three different MRPs shows significant sequence similarities to known ribosomal proteins. In one case, the corresponding human genomic DNA sequences were found in the data bases, and the exon/intron structure was determined.
Keywords:	Amino Acid Sequence, Amino Acid Sequence Homology, Exons, Introns, Molecular Sequence Data, Multidrug Resistance-Associated Proteins, Open Reading Frames, Polyacrylamide Gel Electrophoresis, Ribosomal Proteins, Animals, Cattle, Mice, Rats
Source:	Journal of Biological Chemistry
ISSN:	0021-9258
Publisher:	American Society for Biochemistry and Molecular Biology
Volume:	275
Number:	24
Page Range:	18153-18159
Date:	16 June 2000
Official Publication:	https://doi.org/10.1074/jbc.M909762199
PubMed:	View item in PubMed

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