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Originally published In Press as doi:10.1074/jbc.M109759200 on November 8, 2001

J. Biol. Chem., Vol. 277, Issue 3, 1762-1769, January 18, 2002
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The N-terminal Domain of Mammalian Lysyl-tRNA Synthetase Is a Functional tRNA-binding Domain*

Mathilde Francin, Monika KaminskaDagger , Pierre Kerjan, and Marc Mirande§

From the Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 1 Avenue de la Terrasse, 91190 Gif-sur-Yvette, France

Lysyl-tRNA synthetase from higher eukaryotes possesses a lysine-rich N-terminal polypeptide extension appended to a classical prokaryotic-like LysRS domain. Band shift analysis showed that this extra domain provides LysRS with nonspecific tRNA binding properties. A N-terminally truncated derivative of LysRS, LysRS-Delta N, displayed a 100-fold lower apparent affinity for tRNA3Lys and a 3-fold increase in Km for tRNA3Lys in the aminoacylation reaction, as compared with the native enzyme. The isolated N-domain of LysRS also displayed weak affinity for tRNA, suggesting that the catalytic and N-domains of LysRS act synergistically to provide a high affinity binding site for tRNA. A more detailed analysis revealed that LysRS binds and specifically aminoacylates an RNA minihelix mimicking the amino acid acceptor stem-loop structure of tRNA3Lys, whereas LysRS-Delta N did not. As a consequence, merging an additional RNA-binding domain into a bacterial-like LysRS increases the catalytic efficiency of the enzyme, especially at the low concentration of deacylated tRNA prevailing in vivo. Our results provide new insights into tRNALys channeling in eukaryotic cells and shed new light on the possible requirement of native LysRS for triggering tRNA3Lys packaging into human immunodeficiency virus, type 1 viral particles.

* This work was supported by grants from the Agence Nationale de Recherche sur le SIDA, the Association pour la Recherche sur le Cancer, and La Ligue.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.

Dagger Supported in part by grants from the Jumelage Franco-Polonais program from CNRS. Present address: Inst. of Bioorganic Chemistry, Polish Academy of Sciences, 60-704 Poznan, Poland.

§ To whom correspondence should be addressed. Tel.: 33-1-69-82-35-05; Fax: 33-1-69-82-31-29; E-mail: mirande@lebs.cnrs-gif.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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