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J. Biol. Chem., Vol. 281, Issue 20, 13865-13868, May 19, 2006

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Tandemly Activated tRNAs as Participants in Protein Synthesis^*

From the Departments of Chemistry and Biology, University of Virginia, Charlottesville, Virginia 22904

While all studies of protein synthesis to date have employed monoaminoacylated transfer RNAs, there have been reports that bisphenylalanyl-tRNA is formed by Thermus thermophilus phenylalanyl-tRNA synthetase. Such tandemly activated tRNAs have now been prepared by chemicoenzymatic techniques and are shown to function in both prokaryotic and mammalian protein synthesizing systems. They exhibit characteristics consistent with their possible utility under extreme conditions in natural systems and have important potential advantages for protein elaboration in cell free systems. Mechanistically, the bisaminoacylated tRNAs bind to the ribosomal A-site and utilize the aminoacyl moiety attached to the 3'-position of the terminal adenosine for addition to the growing polypeptide chain. Following translocation to the P-site and transfer of the formed peptidyl moiety, the donor tRNA dissociates from the ribosome as a monoaminoacylated tRNA capable of functioning in a subsequent polypeptide elongation step.

Received for publication, February 7, 2006 , and in revised form, March 20, 2006.

^* This work was supported by National Institutes of Health Grant CA77359, awarded by the NCI. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental data, Fig. 1, and Refs. 1–10.

¹ To whom correspondence should be addressed: Dept. of Chemistry, University of Virginia, McCormick Road, P. O. Box 400319, Charlottesville, VA 22904. Tel.: 434-924-3906; Fax: 434-924-7856; E-mail: sidhecht{at}virginia.edu.

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