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The primer tRNA for reverse transcription in HIV-1, tRNA Lys3 , is selectively packaged into the virus during its assembly, and annealed to the viral genomic RNA. The ribonucleoprotein complex that is involved in the packaging and annealing of tRNA Lys  into HIV-1 consists of Gag, GagPol, tRNA Lys , lysyl-tRNA synthetase (LysRS), and viral genomic RNA. Gag targets tRNA Lys  for viral packaging through Gag's interaction with LysRS, a tRNA Lys -binding protein, while reverse transcriptase (RT) sequences within GagPol (the thumb domain) bind to tRNA Lys . The further annealing of tRNA Lys3  to viral RNA requires nucleocapsid (NC) sequences in Gag, but not the NC sequences GagPol. In this report, we further show that while the RT connection domain in GagPol is not required for tRNA Lys3  packaging into the virus, it is required for tRNA Lys3  annealing to the viral RNA genome.

The connection domain in reverse transcriptase facilitates the in vivo annealing of tRNALys3 to HIV-1 genomic RNA.