Abstract
The leader peptide regulation of the Escherichia coli tryptophanase operon tnaC has a stop codon at position 25 that yields a 24-residue peptide in the absence of inducer. However, in the presence of tryptophan, the leader peptide stays attached to the stalled ribosome as a peptidyl tRNA, and termination is blocked. By altering codons and spacing between codons in the leader peptide, Gong and Yanofsky (see the Perspective by Sachs and Geballe) show that the sequence of the nascent peptide can regulate the translating ribosome, perhaps by creating a ribosome binding site for free tryptophan. Hence, peptides are not only products of translation, but they can also control ribosome movement during translation. F. Gong, C. Yanofsky, Instruction of translating ribosome by nascent peptide. Science 297 , 1864-1867 (2002). [Abstract] [Full Text] M. S. Sachs, A. P. Geballe, Sense and sensitivity--Controlling the ribosome. Science 297 , 1820-1821 (2002). [Abstract] [Full Text]
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