
An open reading frame encoding a member of the L16 family of ribosomal proteins is adjacent to the URA7 gene on the left arm of chromosome II in Saccharomyces cerevisiae. The predicted L16-like polypeptide is basic (pl 11.12), contains 232 amino acids (26.52 kDa) and has 36% amino acid sequence identity to E. coli L16. Immunoblot analysis with polyclonal antibodies to the L16-like polypeptide showed specific cross-reaction with a 22,000 Mr mitochondrial polypeptide that co-sediments with the large subunit of the mitochondrial ribosome in sucrose density gradients. The levels of the L16 mRNA and protein varied in response to carbon source. In [rho degree] cells lacking mitochondrial rRNA, the L16 mRNA accumulated at normal levels, but the protein was barely detectable, indicating RNA-dependent accumulation of the L16 protein. Gene disruption experiments demonstrated that the yeast mitochondrial L16 is an essential ribosomal protein in vivo.
Ribosomal Proteins, Base Sequence, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Genes, Fungal, Molecular Sequence Data, Restriction Mapping, RNA, Fungal, Saccharomyces cerevisiae, Mitochondria, Fungal Proteins, Open Reading Frames, Bacterial Proteins, Mutation, Amino Acid Sequence, RNA, Messenger, Ribosomes, Sequence Alignment
Ribosomal Proteins, Base Sequence, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Genes, Fungal, Molecular Sequence Data, Restriction Mapping, RNA, Fungal, Saccharomyces cerevisiae, Mitochondria, Fungal Proteins, Open Reading Frames, Bacterial Proteins, Mutation, Amino Acid Sequence, RNA, Messenger, Ribosomes, Sequence Alignment
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