Cloning of the Mycoplasma capricolum gene encoding peptide-chain release factor.
In Mycoplasma capricolum (Mc), a relative of Gram+ eubacteria with a high genomic A + T-content, the UGA codon is assigned to Trp instead of being a stop codon. We previously showed the lack of peptide-chain release factor (RF) activity in vitro responding to the UGA codon in this bacterium [Inagaki et al., Nucleic Acids Res. 21 (1993) 1335-1338]. To obtain more information on the translation termination mechanism of Mc, we isolated and sequenced the gene encoding RF. The deduced amino-acid sequence has no RF-2-specific + 1 frameshift site and shows 50 and 36% identity to Escherichia coli RF-1 and RF-2, respectively. We conclude that this gene encodes the putative RF-1 which would possess the conserved 'five-domain' structure of RF family found in various organisms.
Inagaki
Y
Y
Department of Biology, School of Science, Nagoya University, Japan. ug@bio.nagoya-u.ac.jp
Bessho
Y
Y
Hori
H
H
Osawa
S
S
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D009174:Mycoplasma / Q000235:genetics*; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D010454:Peptide Termination Factors / Q000235:genetics*; D017433:Protein Structure, Secondary; D015183:Restriction Mapping
D009838:Oligodeoxyribonucleotides; D010454:Peptide Termination Factors