Identification of a Mammalian Mitochondrial Homolog of Ribosomal Protein S7
Copyright policy )Identification of a Mammalian Mitochondrial Homolog of Ribosomal Protein S7
Bovine mitochondrial small subunit ribosomal proteins were separated by two-dimensional electrophoresis. The region containing the most basic protein(s) was excised and the protein(s) present subjected to in-gel digestion with trypsin. Electrospray tandem mass spectrometry was used to provide sequence information on some of the peptide products. Searches of the human EST database using the sequence of the longest peptide analyzed indicated that this peptide was from the mammalian mitochondrial homolog of prokaryotic ribosomal protein S7 (MRP S7(human)). MRP S7(human) is a 28-kDa protein with a pI of 10. Significant homology to bacterial S7 is observed especially in the C-terminal half of the protein. Surprisingly, MRP S7(human) shows less homology to the corresponding mitochondrial proteins from plants and fungi than to bacterial S7.
- UNC Lineberger Comprehensive Cancer Center United States
- University of North Carolina at Chapel Hill United States
- Research Triangle Park Foundation United States
Expressed Sequence Tags, Ribosomal Proteins, Binding Sites, DNA, Complementary, Base Sequence, Databases, Factual, Molecular Sequence Data, Mass Spectrometry, Peptide Fragments, Mitochondria, Mitochondrial Proteins, Molecular Weight, Bacterial Proteins, RNA, Ribosomal, 16S, Animals, Humans, Cattle, Amino Acid Sequence, Isoelectric Point, Plant Proteins
Expressed Sequence Tags, Ribosomal Proteins, Binding Sites, DNA, Complementary, Base Sequence, Databases, Factual, Molecular Sequence Data, Mass Spectrometry, Peptide Fragments, Mitochondria, Mitochondrial Proteins, Molecular Weight, Bacterial Proteins, RNA, Ribosomal, 16S, Animals, Humans, Cattle, Amino Acid Sequence, Isoelectric Point, Plant Proteins
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