ArticlePloS one2013
The Interaction between tRNA(Lys) 3 and the primer activation signal deciphered by NMR spectroscopy.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Human RPL7 and DDX21 function synergistically with HTLV-1 Gag to overcome genomic RNA structural barriers that block tRNAPro primer annealing.Nucleic acids research · 2026Article
- tRNA modifications in viral replication.The Journal of biological chemistry · 2026Review
- t-RNA mediates provirus deletion in HIV-infected cells.Retrovirology · 2025Article
- Human T-cell leukemia virus type 1 uses a specific tRNARNA (New York, N.Y.) · 2024Article
- The three-way junction structure of the HIV-1 PBS-segment binds host enzyme important for viral infectivity.Nucleic acids research · 2021Article
- NMR Studies of Retroviral Genome Packaging.Viruses · 2020Review
- Overview of the Nucleic-Acid Binding Properties of the HIV-1 Nucleocapsid Protein in Its Different Maturation States.Viruses · 2020Review
- Modulation of the HIV nucleocapsid dynamics finely tunes its RNA-binding properties during virion genesis.Nucleic acids research · 2018Article
- Heterogeneous structures formed by conserved RNA sequences within the HIV reverse transcription initiation site.RNA (New York, N.Y.) · 2016Article
- Insights into the mechanisms of RNA secondary structure destabilization by the HIV-1 nucleocapsid protein.RNA (New York, N.Y.) · 2016Article
- Dynamics of linker residues modulate the nucleic acid binding properties of the HIV-1 nucleocapsid protein zinc fingers.PloS one · 2014Article
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4 authors.
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Abstract
The initiation of reverse transcription of the human immunodeficiency virus type 1 (HIV-1) requires the opening of the three-dimensional structure of the primer tRNA(Lys) 3 for its annealing to the viral RNA at the primer binding site (PBS). Despite the fact that the result of this rearrangement is thermodynamically more stable, there is a high-energy barrier that requires the chaperoning activity of the viral nucleocapsid protein. In addition to the nucleotide complementarity to the PBS, several regions of tRNA(Lys) 3 have been described as interacting with the viral genomic RNA. Among these sequences, a sequence of the viral genome called PAS for "primer activation signal" was proposed to interact with the T-arm of tRNA(Lys) 3, this interaction stimulating the initiation of reverse transcription. In this report, we investigate the formation of this additional interaction with NMR spectroscopy, using a simple system composed of the primer tRNA(Lys) 3, the 18 nucleotides of the PBS, the PAS (8 nucleotides) encompassed or not in a hairpin structure, and the nucleocapsid protein. Our NMR study provides molecular evidence of the existence of this interaction and highlights the role of the nucleocapsid protein in promoting this additional RNA-RNA annealing. This study presents the first direct observation at a single base-pair resolution of the PAS/anti-PAS association, which has been proposed to be involved in the chronological regulation of the reverse transcription.
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