Synthesis of a Chemically Reactive Analog of the Nonsense Codon U-G-A. Its Reaction with Ribosomes of Escherichia coli

Pongs, Olaf; Rössner, Ernst

doi:10.1515/bchm2.1975.356.2.1297

Cited by 5 publications

(1 citation statement)

References 11 publications

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“…Since other codons are recognized by the tRNA anticodon, recognition of peptide chain termination codons involves a different mechanism. The molecular details of RF recognition of nucleic acid sequences have been investigated indirectly by using synthetic modified trinucleotide codons (19), ribosomal structural alterations (1), cross linkage of RF molecules to ribosomal proteins (14) and radioactive termination codons (8). The structure and functional domains of RF molecules have been difficult to identify because of the low number of molecules per cell (about 500 per cell) and the difficulties associated with purification of quantities required for physical and functional study.…”

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confidence: 99%

Cloning of the Escherichia coli release factor 2 gene

Caskey¹,

Forrester²,

Tate³

et al. 1984

J Bacteriol

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The protein release factor 2 (RF2) participates in Escherichia coli polypeptide chain termination with codon specificity (UAA or UGA). A colicin E1 recombinant identified in the Carbon and Clarke E. coli bank contains the protein release factor 2 gene. A 1.7-kilobase E. coli fragment has been subcloned into the plasmid pUC9 vector. Bacterial cells, containing the plasmid recombinant, produce elevated levels of protein release factor 2 as detected by an immune precipitation assay and in vitro measurement of UGA-directed peptide chain termination and [3H]UGA codon recognition.

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confidence: 99%