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Cited by 20RNA and protein synthesis mechanismsHIV Research and TreatmentHIV/AIDS drug development and treatment

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Dual Role for Motif 1 Residues of Human Lysyl-tRNA Synthetase in Dimerization and Packaging into HIV-1

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Dewan, Varun, Wei, Min, Kleiman, Lawrence, Musier-Forsyth, Karin·2012·Journal of Biological Chemistry
DOI 10.1074/jbc.m112.421842PMC PMC3516742
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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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  • The LysRS-Gag interaction has been mapped to the C-terminal domain of the CA region of Gag and the motif 1 dimerization domain of LysRS.

    “This interaction has been mapped to the C-terminal domain of the CA region of Gag and the motif 1 dimerization domain of LysRS (54,55).”

    From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [55]

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Metadata

Authors
Dewan, V., Wei, M., Kleiman, L., & Musier-Forsyth, K.
Affiliations
  • The Ohio State University (US)
  • Jewish General Hospital (CA)
ORCID
Wei, Min
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2012-12
Volume
287
Issue
50
Pages
41955-41962
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.m112.421842
PMC
PMC3516742
OpenAlex
W1974298114
Cited by
20
References
2
Citations by year
2023: 2 · 2022: 1 · 2020: 3 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 3 · 2015: 1 · 2013: 3
FWCI
0.51
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Allergy and Infectious Diseases (R01AI077387, AI077387)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
Keywords
HIV-1, tRNA primer, Gag, tRNA isoacceptors, aminoacylation, oligomerization, reverse transcription
MeSH terms
Humans, Lysine-tRNA Ligase, RNA, Viral, HIV-1, HIV Infections, Fusion Proteins, gag-pol, Virus Assembly, Mutation, Missense, Catalytic Domain, Amino Acid Motifs, gag Gene Products, Human Immunodeficiency Virus, Protein Multimerization, HEK293 Cells

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