Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction

摘要

The translation factor EF-p is required for efficient prokaryotic peptide bond synthesis on 70S ribosomes from fMet-tRNA_f~Met. this protein has been purified from Escherichia coli cells and the gene, efp, encoding it has been cloned and sequenced. We have isolated recombinant clones which overexpress a protein that co-migrates with purigied EF-P upon SDS-PAGE analysis. Using these clones, we report the purification, crystallization and initial characterization of the efp gene product.