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J. Biol. Chem., Vol. 278, Issue 30, 27672-27680, July 25, 2003

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Various Effects of Paromomycin on tmRNA-directed trans-Translation^*

Toshiharu Takahashi  , Takayuki Konno  ¶, Akira Muto  ¶ and Hyouta Himeno  ¶ ||

From the ^¶Department of Biochemistry and Biotechnology, Faculty of Agriculture and Life Science and the Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036-8561 Japan

trans-Translation is an unusual translation in which tmRNA plays a dual function as a tRNA and an mRNA to relieve the stalled translation on the ribosome. In this study, we examined the effects of an aminoglycoside antibiotic, paromomycin, on several tmRNA-related events in vitro. The results of a chemical footprinting study indicated that paromomycin molecules bind tmRNA at G³³²/G³³³ in the tRNA domain and A³¹⁶ in the middle of the long helix between tRNA and mRNA domains. Paromomycin bound at G³³²/G³³³ inhibited aminoacylation, and the inhibition was suppressed by the addition of SmpB, a tmRNA-binding protein. It was also found that paromomycin causes a shift of the translation resuming point on tmRNA by –1. The effect on initiation shift was canceled by a mutation at the paromomycin-binding site in 16 S rRNA but not by mutations in tmRNA. A high concentration of paromomycin inhibited trans-translation, whereas it enhanced the initiation-shifted trans-translation when SmpB was exogenously added or a mutation was introduced at 333. The effect of paromomycin on trans-translation differs substantially from that on canonical translation, in which it induces miscoding by modulating the A site of the decoding helix of the small subunit RNA of the ribosome.

Received for publication, November 18, 2002 , and in revised form, May 3, 2003.

^* This work was supported by Grants-in-aid for Scientific Research 14035201 and 14014201 (to A. M.) and 14014201, 14035202, and 14037203 (to H. H.) from the Ministry of Education, Science, Sports and Culture, Grants-in-aid for Scientific Research 14380322 (to A. M.) and 14360044 (to H. H.) from the Japan Society for the Promotion of Science, and Human Frontier Science Program Research Grant RG0291/2000-M 100 (to H. H.). 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.

These authors contributed equally to this work.

^|| To whom correspondence should be addressed: Dept. of Biochemistry and Biotechnology, Faculty of Agriculture and Life Science, Hirosaki University, Hirosaki 036-8561 Japan. Fax: 81-172-39-3593; E-mail: himeno{at}cc.hirosaki-u.ac.jp.

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This article has been cited by other articles:

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