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Science 13 September 2002:
Vol. 297. no. 5588, pp. 1864 - 1867
DOI: 10.1126/science.1073997
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Reports

Instruction of Translating Ribosome by Nascent Peptide

Feng Gong, Charles Yanofsky*

Expression of the tryptophanase operon of Escherichia coli is regulated by catabolite repression and tryptophan-induced transcription antitermination. An induction site activated by L-tryptophan is created in the translating ribosome during synthesis of TnaC, the 24-residue leader peptide. Replacing the tnaC stop codon with a tryptophan codon allows tryptophan-charged tryptophan transfer RNA to substitute for tryptophan as inducer. This suggests that the ribosomal A site occupied by the tryptophanyl moiety of the charged transfer RNA is the site of induction. The location of tryptophan-12 of nascent TnaC in the peptide exit tunnel was crucial for induction. These results show that a nascent peptide sequence can influence translation continuation and termination within a translating ribosome.

Department of Biological Sciences, Stanford University, Stanford, CA 94305, USA.
*   To whom correspondence should be addressed. E-mail: yanofsky{at}cmgm.stanford.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)