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Journal of Virology, January 2007, p. 68-73, Vol. 81, No. 1
0022-538X/07/$08.00+0 doi:10.1128/JVI.01267-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

,
Vyacheslav Shalak,
,
Mathilde Francin,¶ and
Marc Mirande*
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 1 Avenue de la Terrasse, 91190 Gif-sur-Yvette, France
Received 15 June 2006/ Accepted 8 October 2006
The primer for reverse transcription of the human immunodeficiency virus type 1 (HIV-1) genome is tRNA3Lys. During assembly of HIV-1 particles, tRNA3Lys is taken up from the host cell along with lysyl-tRNA synthetase (LysRS), the tRNA binding protein that specifically aminoacylates the different tRNALys isoacceptors. In humans, the cytoplasmic and mitochondrial species of LysRS are encoded by a single gene by means of alternative splicing. Here, we show that polyclonal antibodies directed to the full-length cytoplasmic enzyme equally recognized the two enzyme species. We raised antibodies against synthetic peptides that allowed discrimination between the two enzymes and found that mitochondrial LysRS is the only cellular source of LysRS detected in the virions. These results open new routes for understanding the molecular mechanisms involved in the specific packaging of tRNA3Lys into viral particles.
Published ahead of print on 18 October 2006.
These authors contributed equally to this work.
Present address: Institut Pasteur, Unité de Régulation Enzymatique des Activités Cellulaires, 25 Rue du Docteur Roux, 75015 Paris, France.
Present address: Institute of Molecular Biology and Genetics, 150 Acad. Zabolotnogo Street, 03143 Kiev, Ukraine.
¶ Present address: INRA, Unité Biopolymères Interactions Assemblages, Rue de la Géraudière, 44316 Nantes Cedex 03, France.
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