ArticleRNA (New York, N.Y.)2000
NMR and biochemical characterization of recombinant human tRNA(Lys)3 expressed in Escherichia coli: identification of posttranscriptional nucleotide modifications required for efficient initiation of HIV-1 reverse transcription.
Article in RNA (New York, N.Y.), 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- tRNA modifications in viral replication.The Journal of biological chemistry · 2026Review
- Probing the structure of human tRNARSC advances · 2023Article
- Modified Nucleotides for Chemical and Enzymatic Synthesis of Therapeutic RNA.Current medicinal chemistry · 2023Article
- Rational engineering enables co-crystallization and structural determination of the HIV-1 matrix-tRNA complex.STAR protocols · 2022Article
- The nucleic acid chaperone activity of the HIV-1 Gag polyprotein is boosted by its cellular partner RPL7: a kinetic study.Nucleic acids research · 2020Article
- Time-resolved NMR monitoring of tRNA maturation.Nature communications · 2019Article
- Molecular basis for transfer RNA recognition by the double-stranded RNA-binding domain of human dihydrouridine synthase 2.Nucleic acids research · 2019Article
- RNA: packaged and protected by VLPs.RSC advances · 2018Article
- Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae.Scientific reports · 2016Article
- Association of human mitochondrial lysyl-tRNA synthetase with HIV-1 GagPol does not require other viral proteins.Biochimie open · 2016Article
- Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein. Importance of the C-terminal unstructured tail.RNA biology · 2014Article
- Co-expression of RNA-protein complexes in Escherichia coli and applications to RNA biology.Nucleic acids research · 2013Article
- In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya.Nucleic acids research · 2013Article
- The Interaction between tRNA(Lys) 3 and the primer activation signal deciphered by NMR spectroscopy.PloS one · 2013Article
- Fast production of homogeneous recombinant RNA--towards large-scale production of RNA.Nucleic acids research · 2012Article
- Human tRNA(Lys3)(UUU) is pre-structured by natural modifications for cognate and wobble codon binding through keto-enol tautomerism.Journal of molecular biology · 2012Article
- Initiation of HIV Reverse Transcription.Viruses · 2010Article
- The structure of the human tRNALys3 anticodon bound to the HIV genome is stabilized by modified nucleosides and adjacent mismatch base pairs.Nucleic acids research · 2009Article
- A generic protocol for the expression and purification of recombinant RNA in Escherichia coli using a tRNA scaffold.Nature protocols · 2009Article
- Complementation of human immunodeficiency virus type 1 replication by intracellular selection of Escherichia coli formula supplied in trans.Journal of virology · 2006Article
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5 authors.
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Abstract
Reverse transcription of HIV-1 viral RNA uses human tRNA(Lys)3 as a primer. Some of the modified nucleotides carried by this tRNA must play a key role in the initiation of this process, because unmodified tRNA produced in vitro is only marginally active as primer. To provide a better understanding of the contribution of base modifications in the initiation complex, we have designed a recombinant system that allows tRNA(Lys)3 expression in Escherichia coli. Because of their high level of overexpression, some modifications are incorporated at substoichiometric levels. We have purified the two major recombinant tRNA(Lys)3 subspecies, and their modified nucleotide contents have been characterized by a combination of NMR and biochemical techniques. Both species carry psis, Ds, T, t6A, and m7G. Differences are observed at position 34, within the anticodon. One fraction lacks the 5-methylaminomethyl group, whereas the other lacks the 2-thio group. Although the s2U34-containing recombinant tRNA is a less efficient primer, it presents most of the characteristics of the mammalian tRNA. On the other hand, the mnm5U34-containing tRNA has a strongly reduced activity. Our results demonstrate that the modifications that are absent in E. coli (m2G10, psi27, m5C48, m5C49, and m1A58) as well as the mnm5 group at position 34 are dispensable for initiation of reverse transcription. In contrast, the 2-thio group at position 34 seems to play an important part in this process.
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