ArticleThe Journal of biological chemistry2012
Dual role for motif 1 residues of human lysyl-tRNA synthetase in dimerization and packaging into HIV-1.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- Aminoacyl-tRNA synthetase interactions in SARS-CoV-2 infection.Biochemical Society transactions · 2023Review
- Review
- 3-Dimensional architecture of the human multi-tRNA synthetase complex.Nucleic acids research · 2020Article
- Article
- Roles of aminoacyl-tRNA synthetases in immune regulation and immune diseases.Cell death & disease · 2019Review
- Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication.The Journal of biological chemistry · 2019Review
- Characterization of association of human mitochondrial lysyl-tRNA synthetase with HIV-1 Pol and tRNABMC biochemistry · 2018Article
- The role of tRNA synthetases in neurological and neuromuscular disorders.FEBS letters · 2018Review
- HIV-1 Exploits a Dynamic Multi-aminoacyl-tRNA Synthetase Complex To Enhance Viral Replication.Journal of virology · 2017Article
- HMGB1 Activates Proinflammatory Signaling via TLR5 Leading to Allodynia.Cell reports · 2016Article
- On the Selective Packaging of Genomic RNA by HIV-1.Viruses · 2016Review
- Evolutionary Limitation and Opportunities for Developing tRNA Synthetase Inhibitors with 5-Binding-Mode Classification.Life (Basel, Switzerland) · 2015Review
- [New aspects on the pathogenesis of myositis].Zeitschrift fur Rheumatologie · 2013Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The primer for reverse transcription in human immunodeficiency virus type 1, human tRNA(Lys,3), is selectively packaged into the virion along with tRNA(Lys1,2). Human lysyl-tRNA synthetase (hLysRS), the only cellular factor known to interact specifically with all three tRNA(Lys) isoacceptors, is also selectively packaged into HIV-1. We have previously defined a tRNA(Lys) packaging complex that includes the tRNA(Lys) isoacceptors, LysRS, HIV-1 Gag, GagPol, and viral RNA. Numerous studies support the hypothesis that during tRNA(Lys) packaging, a Gag·GagPol complex interacts with a tRNA(Lys)·LysRS complex, with Gag interacting specifically with the catalytic domain of LysRS, and GagPol interacting with both Gag and tRNA(Lys). In this work, we have identified residues along one face of the motif 1 dimerization helix (H7) of hLysRS that are critical for packaging of the synthetase into virions. Mutation of these residues affects binding to Gag in vitro, as well as the oligomerization state and aminoacylation activity of the synthetase. Taken together, these data suggest that H7 of LysRS has a dual function. In its canonical role it maintains the synthetase dimer interface, whereas in its function in tRNA primer recruitment, it bridges interactions with HIV-1 Gag.
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