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Originally published In Press as doi:10.1074/jbc.M005043200 on November 1, 2000

J. Biol. Chem., Vol. 276, Issue 4, 2387-2394, January 26, 2001
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tRNA Recognition of tRNA-guanine Transglycosylase from a Hyperthermophilic Archaeon, Pyrococcus horikoshii*

Masakatsu WatanabeDagger §, Nobukazu NamekiDagger §, Mami Matsuo-TakasakiDagger , Susumu Nishimura||, and Norihiro OkadaDagger **

From the Dagger  Department of Biological Sciences, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8501 and the || Banyu Tsukuba Research Institute (Merck), 3 Ookubo, Tsukuba 300-2611, Japan

In the biosynthesis of archaeosine, archaeal tRNA-guanine transglycosylase (TGT) catalyzes the replacement of guanine at position 15 in the D loop of most tRNAs by a free precursor base. We examined the tRNA recognition of TGT from a hyperthermophilic archaeon, Pyrococcus horikoshii. Mutational studies using variant tRNAVal transcripts revealed that both guanine and its location (position 15) were strictly recognized by TGT without any other sequence-specific requirements. It appeared that neither the global L-shaped structure of a tRNA nor the local conformation of the D loop contributed to recognition by TGT. A minihelix composed of the acceptor stem and D arm of tRNAVal, designed as a potential minimal substrate, failed to serve as a substrate for TGT. Only a minihelix with mismatched nucleotides at the junction between the two domains served as a good substrate, suggesting that mismatched nucleotides in the helix provide the specific information that allows TGT to recognize the guanine in the D loop. Our findings indicate that the tRNA recognition requirements of P. horikoshii TGT are sufficiently limited and specific to allow the enzyme to recognize efficiently any tRNA species whose structure is not fully stabilized in an extremely high temperature environment.

* This work was supported by a grant-in-aid for scientific research on priority areas from the Ministry of Education, Science and Culture, Japan (to N. O.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These two authors contributed equally to this work.

Present address: Dept. of Industrial Chemistry, Chiba Institute of Technology, Chiba 275-0016, Japan.

** To whom correspondence should be addressed: Tel.: 81-45-924-5742; Fax: 81-45-924-5835; E-mail: nokada@bio.titech.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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