ArticleNucleic acids research2017
Pausing kinetics dominates strand-displacement polymerization by reverse transcriptase.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Optimising DNA origami assembly by reducing off-target interactions.Nature communications · 2026Article
- Engineering a Mechanoresponsive DNA Origami Capsule for Drug Delivery to Narrowed Arteries.Nano letters · 2026Article
- Intrinsically disordered regions facilitate target search to drive promoter selectivity by a yeast transcription factor.Nature communications · 2025Article
- Efficient circRNA Detection Using the Processive Reverse Transcriptase uMRT.Bio-protocol · 2025Article
- Characterization and implementation of the MarathonRT template-switching reaction to expand the capabilities of RNA-seq.RNA (New York, N.Y.) · 2024Article
- Kinetics of elementary steps in loop-mediated isothermal amplification (LAMP) show that strand invasion during initiation is rate-limiting.Nucleic acids research · 2023Article
- Single molecule characterization of the binding kinetics of a transcription factor and its modulation by DNA sequence and methylation.Nucleic acids research · 2021Article
- MrHAMER yields highly accurate single molecule viral sequences enabling analysis of intra-host evolution.Nucleic acids research · 2021Article
- Temperature controlled high-throughput magnetic tweezers show striking difference in activation energies of replicating viral RNA-dependent RNA polymerases.Nucleic acids research · 2020Article
- Template-switching mechanism of a group II intron-encoded reverse transcriptase and its implications for biological function and RNA-Seq.The Journal of biological chemistry · 2019Article
- The base pair-scale diffusion of nucleosomes modulates binding of transcription factors.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Single-molecule DNA unzipping reveals asymmetric modulation of a transcription factor by its binding site sequence and context.Nucleic acids research · 2018Article
- The mechano-chemistry of a monomeric reverse transcriptase.Nucleic acids research · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reverse transcriptase (RT) catalyzes the conversion of the viral RNA into an integration-competent double-stranded DNA, with a variety of enzymatic activities that include the ability to displace a non-template strand concomitantly with polymerization. Here, using high-resolution optical tweezers to follow the activity of the murine leukemia Virus RT, we show that strand-displacement polymerization is frequently interrupted. Abundant pauses are modulated by the strength of the DNA duplex ∼8 bp ahead, indicating the existence of uncharacterized RT/DNA interactions, and correspond to backtracking of the enzyme, whose recovery is also modulated by the duplex strength. Dissociation and reinitiation events, which induce long periods of inactivity and are likely the rate-limiting step in the synthesis of the genome in vivo, are modulated by the template structure and the viral nucleocapsid protein. Our results emphasize the potential regulatory role of conserved structural motifs, and may provide useful information for the development of potent and specific inhibitors.
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