By evaluating the kinetics of radioactive labelling of nascent and finished polypeptides, the peptide-chain elongation rate for Escherichia coli B/r at three different growth rates (mu) was determined to be 17 amino acids/s for the fast-growing cells (mu equals 1.3 and 2.0 doublings/h) and 12 amino acids/s for slow-growing cells (mu equals 0.67 doublings/h). The results agree with the growth-rate-dependence of the rate of peptide-chain elongation found for the translation of newly induced β-galactosidase messenger in this strain and under these conditions of growth [Dalbow & Young (1975) Biochem. J. 150, 13-20]. Together with the previously observed ribosome efficiency at these growth rates [Dennis & Bremer (1974) J. Mol. Biol. 84, 407-422] the results indicate that the fraction of ribosomes engaged in protein synthesis is about 0.8 at all three growth rates.
Research Article| November 15 1976
Polypeptide-chain-elongation rate in Escherichia coli B/r as a function of growth rate
Biochem J (1976) 160 (2): 185–194.
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R Young, H Bremer; Polypeptide-chain-elongation rate in Escherichia coli B/r as a function of growth rate. Biochem J 15 November 1976; 160 (2): 185–194. doi: https://doi.org/10.1042/bj1600185
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