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Papers In Press, published online ahead of print November 8, 2001
J. Biol. Chem, 10.1074/jbc.M109759200
Submitted on October 9, 2001
Revised on November 8, 2001
Accepted on November 8, 2001

The N-domain of mammalian lysyl-tRNA synthetase is a functional tRNA binding domain

Mathilde Francin, Monika Kaminska, Pierre Kerjan, and Marc Mirande

L.E.B.S., Gif-sur-Yvette 91190

Corresponding Author: Marc.Mirande{at}lebs.cnrs-gif.fr

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 non specific 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 to triggering tRNA3Lys packaging into HIV-1 viral particles.


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