Affiliation:
1. Department of Biochemistry, University of Washington, Seattle, Washington 98195
Abstract
The rate of polypeptide chain elongation during steady-state, polyamine-limited growth of a mutant of
Escherichia coli
was measured by two independent techniques. Analysis of polysome patterns gave values of 17.5 and 9.5 amino acids per s at 37 C in unstarved and polyamine-limited cells, respectively. From the kinetics of entry of labeled amino acids into polypeptides of defined molecular weights, values at 30 C of 10.1 and 5.8 amino acids per s were obtained for unstarved and polyamine-limited cultures, respectively. Correction of these values to 37 C resulted in rates of 15.0 and 8.7 amino acids per s. These results support the previous conclusion, based on the kinetics of β-galactosidase induction, that polyamine starvation decreases the rate of protein synthesis by limiting the velocity of polypeptide chain elongation.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
20 articles.
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