Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis
| Autor: | Koichi Ito, Makiko Uno, Yoshikazu Nakamura, Kanae Ebihara |
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| Rok vydání: | 1996 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Protein Conformation Molecular Sequence Data Saccharomyces cerevisiae Biology Models Biological Ribosome Fungal Proteins RNA Transfer Phe Xenopus laevis Eukaryotic translation RNA Transfer Prokaryotic release factors Schizosaccharomyces Prokaryotic translation Animals Humans Eukaryotic release factors Amino Acid Sequence Prokaryotic initiation factor Conserved Sequence Genetics Multidisciplinary Bacteria Sequence Homology Amino Acid Peptide Termination Factors Peptide Chain Termination Translational Peptide Elongation Factor G Peptide Elongation Factors Stop codon Models Structural Biochemistry Nucleic Acid Conformation Ribosomes Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 93:5443-5448 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.93.11.5443 |
| Popis: | Translation termination requires two codon-specific polypeptide release factors in prokaryotes and one omnipotent factor in eukaryotes. Sequences of 17 different polypeptide release factors from prokaryotes and eukaryotes were compared. The prokaryotic release factors share residues split into seven motifs. Conservation of many discrete, perhaps critical, amino acids is observed in eukaryotic release factors, as well as in the C-terminal portion of elongation factor (EF) G. Given that the C-terminal domains of EF-G interacts with ribosomes by mimicry of a tRNA structure, the pattern of conservation of residues in release factors may reflect requirements for a tRNA-mimicry for binding to the A site of the ribosome. This mimicry would explain why release factors recognize stop codons and suggests that all prokaryotic and eukaryotic release factors evolved from the progenitor of EF-G. |
| Databáze: | OpenAIRE |
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