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Originally published In Press as doi:10.1074/jbc.M105150200 on September 27, 2001

J. Biol. Chem., Vol. 276, Issue 50, 46770-46778, December 14, 2001
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Dual Mode Recognition of Two Isoacceptor tRNAs by Mammalian Mitochondrial Seryl-tRNA Synthetase*

Nobukazu ShimadaDagger , Tsutomu SuzukiDagger §, and Kimitsuna WatanabeDagger §

From the Dagger  Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656 and the § Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8583, Japan

Animal mitochondrial translation systems contain two serine tRNAs, corresponding to the codons AGY (Y = U and C) and UCN (N = U, C, A, and G), each possessing an unusual secondary structure; tRNA<UP><SUB>GCU</SUB><SUP>Ser</SUP></UP> (for AGY) lacks the entire D arm, whereas tRNA<UP><SUB>UGA</SUB><SUP>Ser</SUP></UP> (for UCN) has an unusual cloverleaf configuration. We previously demonstrated that a single bovine mitochondrial seryl-tRNA synthetase (mt SerRS) recognizes these topologically distinct isoacceptors having no common sequence or structure. Recombinant mt SerRS clearly footprinted at the TPsi C loop of each isoacceptor, and kinetic studies revealed that mt SerRS specifically recognized the TPsi C loop sequence in each isoacceptor. However, in the case of tRNA<UP><SUB>UGA</SUB><SUP>Ser</SUP></UP>, TPsi C loop-D loop interaction was further required for recognition, suggesting that mt SerRS recognizes the two substrates by distinct mechanisms. mt SerRS could slightly but significantly misacylate mitochondrial tRNAGln, which has the same TPsi C loop sequence as tRNA<UP><SUB>UGA</SUB><SUP>Ser</SUP></UP>, implying that the fidelity of mitochondrial translation is maintained by kinetic discrimination of tRNAs in the network of aminoacyl-tRNA synthetases.

* This work was supported by a grant-in-aid for scientific research on priority areas from the Ministry of Education, Culture, Sports, Science and Technology (Japan).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.

To whom correspondence should be addressed. Tel.: 81-471-36-3601; Fax: 81-471-36-3600; E-mail: kw@kwl.t.u-tokyo.ac.jp.

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