Cloning of the Escherichia coli release factor 2 gene

C. T. Caskey, W. C. Forrester, W. Tate, C. D. Ward

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)365-368
Number of pages4
JournalJournal of Bacteriology
Volume158
Issue number1
StatePublished - Jan 1 1984

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ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Caskey, C. T., Forrester, W. C., Tate, W., & Ward, C. D. (1984). Cloning of the Escherichia coli release factor 2 gene. Journal of Bacteriology, 158(1), 365-368.