Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 17 September 2002
Vol. 2002, Issue 150, p. tw340
[DOI: 10.1126/stke.2002.150.tw340]

EDITORS' CHOICE

Translation Ribosome Regulation by Protein Products

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]

Citation: Ribosome Regulation by Protein Products. Sci. STKE 2002, tw340 (2002).



To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882