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- W2049252219 endingPage "32259" @default.
- W2049252219 startingPage "32254" @default.
- W2049252219 abstract "Elongation factor P (EFP) is a protein that stimulates the peptidyltransferase activity of fully assembled 70 S prokaryotic ribosomes and enhances the synthesis of certain dipeptides initiated by N-formylmethionine. This reaction appears conserved throughout species and is promoted in eukaryotic cells by a homologous protein, eIF5A. Here we ask whether the Escherichia coli gene encoding EFP is essential for cell viability. A kanamycin resistance (Kan R) gene was inserted near the N-terminal end of the efp gene and was cloned into a plasmid, pMAK705, that has a temperature-sensitive origin of replication. After transformation into a recA+ E. coli strain, temperature-sensitive mutants were isolated, and their chromosomal DNA was sequenced. Mutants containing the efp-Kan R gene in the chromosome grew at 33 °C only in the presence of the wild-type copy of the efp gene in the pMAK705 plasmid and were unable to grow at 44 °C. Incorporation of various isotopes in vivo suggests that translation is impaired in the efp mutant at 44 °C. At 44 °C, mutant cells are severely defective in peptide-bond formation. We conclude that the efp gene is essential for cell viability and is required for protein synthesis." @default.
- W2049252219 created "2016-06-24" @default.
- W2049252219 creator A5029523917 @default.
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- W2049252219 creator A5074420539 @default.
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- W2049252219 date "1997-12-01" @default.
- W2049252219 modified "2023-10-13" @default.
- W2049252219 title "The Gene Encoding the Elongation Factor P Protein Is Essential for Viability and Is Required for Protein Synthesis" @default.
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- W2049252219 doi "https://doi.org/10.1074/jbc.272.51.32254" @default.
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