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In vitro Synthesis of the Tryptophan Operon Leader Peptides of Escherichia coli, Serratia marcescens, and Salmonella typhimurium

Anathbandhu Das, Joseph Urbanowski, Herbert Weissbach, John Nestor and Charles Yanofsky
Proceedings of the National Academy of Sciences of the United States of America
Vol. 80, No. 10, [Part 1: Biological Sciences] (May 15, 1983), pp. 2879-2883
Stable URL: http://www.jstor.org/stable/13676
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
In vitro Synthesis of the Tryptophan Operon Leader Peptides of Escherichia coli, Serratia marcescens, and Salmonella typhimurium
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Abstract

We used an in vitro DNA-dependent protein-synthesizing system to demonstrate de novo synthesis of the leader peptide specified by the tryptophan (trp) operons of several bacterial species. Peptide synthesis was directed by self-ligated short restriction fragments containing the trp promoter and leader regions. Synthesis of leader peptides was established by demonstrating that they were labeled in vitro only by those amino acids predicted to be present in the peptides. Leader peptide synthesis was abolished by the addition of the Escherichia coli trp repressor. The E. coli trp leader peptide was found to be extremely labile in vitro; it had a half-life of 3-4 min. In a highly purified DNA-dependent peptide-synthesizing system, synthesis of the di- and tripeptides predicted from the Salmonella typhimurium trp operon leader sequence, fMet-Ala and fMet-Ala-Ala, also was observed. Using this dipeptide synthesis system, we demonstrated that translation initiation at the ribosome binding site used for trp leader peptide synthesis was reduced 10-fold when the transcript contained a segment complementary to the ribosome binding site.

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