| http://purl.uniprot.org/citations/795670 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/795670 | http://www.w3.org/2000/01/rdf-schema#comment | "A recently identified soluble protein, named EF-P, stimulates peptide bond synthesis from ribosomal-bound N-formylmethionyl-tRNA and the aminoacyl-tRNA analog, puromycin. Using this model of peptide bond formation we have purified this activity approximately 100-fold from ribosome-free extracts of Escherichia coli. In order to study the mechanism by which the EF-P factor stimulates peptide bond formation, we examined and compared the requirements and site of action of the spontaneous and the EF-P-mediated synthesis of peptide bonds. We find that "enzymic" peptide bond synthesis (+EF-P) is characterized by relatively broad temperature and NH4Cl optima, a sharp Mg2+ optimum at 12 mM, and an apparent pKa of approximately 8.5. The characteristics of enzymic peptide bond synthesis closely resemble those reported for native peptidyl-puromycin formation rather than other models of peptide synthesis. Factor EF-P requires both 30-S and 50-S subunits for activity. The 30-S particle is inactive by itself and may function in the reaction merely to bind the fMet-tRNA substrate. Both the peptidyl transferase and the EF-P binding site may be part of the 50-S subunit. Unlike all other propagation factors, EF-P does not require the 50-S ribosomal proteins L7 and L12 and may therefore occupy a different ribosomal site."xsd:string |
| http://purl.uniprot.org/citations/795670 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1976.tb11137.x"xsd:string |
| http://purl.uniprot.org/citations/795670 | http://purl.uniprot.org/core/author | "Glick B.R."xsd:string |
| http://purl.uniprot.org/citations/795670 | http://purl.uniprot.org/core/author | "Ganoza M.C."xsd:string |
| http://purl.uniprot.org/citations/795670 | http://purl.uniprot.org/core/date | "1976"xsd:gYear |
| http://purl.uniprot.org/citations/795670 | http://purl.uniprot.org/core/name | "Eur J Biochem"xsd:string |
| http://purl.uniprot.org/citations/795670 | http://purl.uniprot.org/core/pages | "483-491"xsd:string |
| http://purl.uniprot.org/citations/795670 | http://purl.uniprot.org/core/title | "Characterization and site of action of a soluble protein that stimulates peptide-bond synthesis."xsd:string |
| http://purl.uniprot.org/citations/795670 | http://purl.uniprot.org/core/volume | "71"xsd:string |
| http://purl.uniprot.org/citations/795670 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/795670 |
| http://purl.uniprot.org/citations/795670 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/795670 |
| http://purl.uniprot.org/uniprot/#_P0A6N4-mappedCitation-795670 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/795670 |
| http://purl.uniprot.org/uniprot/P0A6N4 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/795670 |