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J. Biol. Chem., Vol. 277, Issue 20, 17389-17396, May 17, 2002

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Correlation Between tRNA^Lys3 Aminoacylation and Its Incorporation into HIV-1^*

Hassan Javanbakht^§, Shan Cen, Karin Musier-Forsyth^¶, and Lawrence Kleiman^§**

From the  Lady Davis Institute for Medical Research and McGill AIDS Centre, Jewish General Hospital, Departments of ^§ Medicine and  Microbiology and Immunology, McGill University, Montreal, Quebec H3T 1E2, Canada and the ^¶ Department of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455

During human immunodeficiency virus type 1 (HIV-1) assembly, tRNA^Lys is selectively packaged into the virus, where tRNA^Lys3 serves as the primer for reverse transcription. Lysyl-tRNA synthetase is also selectively incorporated into HIV-1 and is therefore a strong candidate for being the signal by which viral proteins interact with tRNA^Lys isoacceptors. Previously, mutations in the tRNA^Lys3 anticodon have been shown to strongly inhibit the charging of tRNA^Lys3 by lysyl-tRNA synthetase in vitro, and we show here that in vivo aminoacylation is also inhibited by anticodon changes. The order of decreasing in vivo aminoacylation for tRNA^Lys3 anticodon mutants is: wild-type SUU (where S = mcm⁵S²U) 100%)  SGU (49%)  CGU (40%)  SGA (0%) and CGA (0%). We found that the ability of these tRNA^Lys3 anticodon variants to be aminoacylated in vivo is directly correlated with their ability to be packaged into HIV-1. These data showed that the anticodon is a major determinant for tRNA^Lys3 packaging and support the conclusion that its productive interaction with lysyl-tRNA synthetase is important for tRNA^Lys3 incorporation into HIV-1.

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