PMID:1408743

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Citation

Pel, HJ, Rep, M and Grivell, LA (1992) Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure. Nucleic Acids Res. 20:4423-8

Abstract

We have recently reported the cloning and sequencing of the gene for the mitochondrial release factor mRF-1. mRF-1 displays high sequence similarity to the bacterial release factors RF-1 and RF-2. A database search for proteins resembling these three factors revealed high similarities to two amino acid sequences deduced from unassigned genomic reading frames in Escherichia coli and Bacillus subtilis. The amino acid sequence derived from the Bacillus reading frame is 47% identical to E.coli and Salmonella typhimurium RF-2, strongly suggesting that it represents B.subtilis RF-2. Our comparison suggests that the expression of the B.subtilis gene is, like that of the E.coli and S. typhimurium RF-2 genes, autoregulated by a stop codon dependent +1 frameshift. A comparison of prokaryotic and mitochondrial release factor sequences, including the putative B.subtilis RF-2, leads us to propose a five-domain model for release factor structure. Possible functions of the various domains are discussed.

Links

PubMed PMC334167

Keywords

Amino Acid Sequence; Bacillus subtilis/chemistry; Bacillus subtilis/genetics; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Base Sequence; Escherichia coli/chemistry; Escherichia coli/genetics; Fungal Proteins/chemistry; Fungal Proteins/genetics; Mitochondria/metabolism; Molecular Sequence Data; Peptide Termination Factors/chemistry; Peptide Termination Factors/genetics; Protein Conformation; Saccharomyces cerevisiae/chemistry; Saccharomyces cerevisiae/genetics

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