Cloning, sequencing and over-expression of the gene for prokaryotic factor EF-P involved in peptide bond synthesis

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DOIResolve DOI: http://doi.org/10.1093/nar/19.22.6215
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TypeArticle
Journal titleNucleic Acids Research
Volume19
Issue22
Pages62156220; # of pages: 6
AbstractA soluble protein EF-P (elongation factor P) from Escherichia coli has been purified and shown to stimulate efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Based on the partial amino acid sequence of EFP, 18- and 24-nucleotide DNA probes were synthesized and used to screen λ phage clones from the Kohara Gene Bank. The entire EF-P gene was detected on λ clone #650 which contains sequences from the 94 minute region of the E.coli genome. Two DNA fragments, 3.0 and 0.78 kilobases in length encompassing the gene, were isolated and cloned into pUC18 and pUC19. Partially purified extracts from cells transformed with these plasmids overrepresented a protein which co-migrates with EF-P upon SDS polyacrylamide gel electrophoresis, and also exhibited increased EF-P mediated peptide-bond synthetic activity. Based on DNA sequence analysis of this gene, the EF-P protein consists of 187 amino acids with a calculated molecular weight of 20,447. The sequence and chromosomal location of EF-P establishes it as a unique gene product.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NRC numberAOKI1991
NPARC number9376053
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Record identifier1fdaf18e-9ba5-4298-966f-d1f84b4622d7
Record created2009-07-10
Record modified2016-05-09
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