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HIV-1 reverse transcription is primed by a cellular tRNAlys3 molecule that binds to the primer binding site (PBS) in the genomic RNA. An additional interaction between the tRNA molecule and the primer activation signal (PAS) is thought to regulate the initiation of reverse transcription. The mechanism of tRNA annealing onto the HIV-1 genome was examined using ensemble and single-molecule Förster Resonance Energy Transfer (FRET) assays, in which fluorescent donor and acceptor molecules were covalently attached to an RNA template mimicking the PBS region. The role of the viral nucleocapsid (NC) protein in tRNA annealing was studied. Both heat annealing and NC-mediated annealing of tRNAlys3 were found to change the FRET efficiency, and thus the conformation of the HIV-1 RNA template. The results are consistent with a model for tRNA annealing that involves an interaction between the tRNAlys3 molecule and the PAS sequence in the HIV-1 genome. The NC protein may stimulate the interaction of the tRNA molecule with the PAS, thereby regulating the initiation of reverse transcription.

Original publication

DOI

10.1261/rna.035733.112

Type

Journal article

Journal

RNA (New York, N.Y.)

Publication Date

04/2013

Volume

19

Pages

517 - 526

Addresses

1Department of Molecular Biology, Aarhus University, Aarhus, Denmark.

Keywords

Humans, HIV-1, RNA, Transfer, Lys, RNA, Viral, Fluorescence Resonance Energy Transfer, Reverse Transcription, Nucleic Acid Conformation, Genome, Viral, Host-Pathogen Interactions