ArticleProceedings of the National Academy of Sciences of the United States of America2020
How a B family DNA polymerase has been evolved to copy RNA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Crystal structure of a closed ternary complex of a HNA Reverse Transcriptase in complex with a HNA/DNA duplex.PloS one · 2026Article
- Engineering a Thermostable Reverse Transcriptase for RT-PCR Through Rational Design ofBiomolecules · 2025Article
- Inhibition of monkeypox polymerase holoenzyme and methyltransferase using bioactive compounds of black tea: a computational approach.Scientific reports · 2025Article
- Structural insights into a DNA polymerase reading the xeno nucleic acid HNA.Nucleic acids research · 2025Article
- Direct Enzyme Engineering of B Family DNA Polymerases for Biotechnological Approaches.Bioengineering (Basel, Switzerland) · 2023Review
- Minimizing amplification bias during reverse transcription for in vitro selections.RNA (New York, N.Y.) · 2023Article
- Thermally controlled intein splicing of engineered DNA polymerases provides a robust and generalizable solution for accurate and sensitive molecular diagnostics.Nucleic acids research · 2023Article
- Structural basis for the assembly of the DNA polymerase holoenzyme from a monkeypox virus variant.Science advances · 2023Article
- Natural History of DNA-Dependent DNA Polymerases: Multiple Pathways to the Origins of DNA.Viruses · 2023Article
- Crystal structures of N-terminally truncated telomerase reverse transcriptase from fungi‡.Nucleic acids research · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
We report here crystal structures of a reverse transcriptase RTX, which was evolved in vitro from the B family polymerase KOD, in complex with either a DNA duplex or an RNA-DNA hybrid. Compared with the apo, binary, and ternary complex structures of the original KOD polymerase, the 16 substitutions that result in the function of copying RNA to DNA do not change the overall protein structure. Only six substitutions occur at the substrate-binding surface, and the others change domain-domain interfaces in the polymerase to enable RNA-DNA hybrid binding and reverse transcription. Most notably, F587L at the Palm and Thumb interface stabilizes the open and apo conformation of the Thumb. The intrinsically flexible Thumb domain seems to play a major role in accommodating the RNA-DNA hybrid product distal to the active site. This is reminiscent of naturally occurring RNA-dependent DNA polymerases, including telomerase, which have a dramatically augmented Thumb domain, and of reverse transcriptase, which extends its Thumb with the RNase H domain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.