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Nucleic Acids Research 2005 33(17):5544-5552; doi:10.1093/nar/gki871
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Published online 4 October 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

Competition between trans-translation and termination or elongation of translation

Krisana Asano1, Daisuke Kurita1, Kazuma Takada2, Takayuki Konno2,3, Akira Muto1,2 and Hyouta Himeno1,2,*

1Department of Biochemistry and Biotechnology, Faculty of Agriculture and Life Science, Hirosaki University Hirosaki 036-8561 2The United Graduate School of Agricultural Sciences, Iwate University Morioka 020-8550 3Department of Microbiology, AKITA Prefectural Institute of Public Health Akita 010-0874, Japan

*To whom correspondence should be addressed. Tel: +81 172 39 3592; Fax: +81 172 39 3593; Email: himeno{at}cc.hirosaki-u.ac.jp

Received July 21, 2005. Revised September 12, 2005. Accepted September 12, 2005.

The effects of tRNA, RF1 and RRF on trans-translation by tmRNA were examined using a stalled complex of ribosome prepared using a synthetic mRNA and pure Escherichia coli translation factors. No endoribonucleolytic cleavage of mRNA around the A site was found in the stalled ribosome and was required for the tmRNA action. When the A site was occupied by a stop codon, alanyl-tmRNA competed with RF1 with the efficiency of peptidyl-transfer to alanyl-tmRNA for trans-translation inversely correlated to the efficiency of translation termination. The competition was not affected by RF3. A sense codon also serves as a target for alanyl-tmRNA with competition of aminoacyl-tRNA. The extent of inhibition was decreased with the length of the 3'-extension of mRNA. RRF, only at a high concentration, slightly affected peptidyl-transfer for trans-translation, although it did not affect the canonical elongation. These results indicate that alanyl-tmRNA does not absolutely require the truncation of mRNA around the A site but prefers an mRNA of a short 3'-extension from the A site and that it can operate on either a sense or termination codon at the A site, at which alanyl-tmRNA competes with aminoacyl-tRNA, RF and RRF.


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