Polypeptide-chain-elongation rate in Escherichia coli B/r as a function of growth rate. Academic Article

abstract

• 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 beta-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.

authors

• Young, Ryland

published proceedings

• Biochem J

author list (cited authors)

• Young, R., & Bremer, H.

citation count

• 146

complete list of authors

• Young, R||Bremer, H

publication date

• January 1976

publisher

• Portland Press  Publisher

published in

• Biochemical Journal  Journal

keywords

• Bacterial Proteins
• Enzyme Induction
• Escherichia Coli
• Galactosidases
• Kinetics
• Models, Biological
• Molecular Weight
• Peptide Chain Elongation, Translational
• Ribosomes

Digital Object Identifier (DOI)

• 10.1042/bj1600185

start page

• 185

end page

• 194

volume

• 160

issue

• 2

URL

• http://dx.doi.org/10.1042/bj1600185