Evidence map›Paper›PMID 28108662›Full record

ArticleNucleic acids research2017

Coordination between the polymerase and RNase H activity of HIV-1 reverse transcriptase.

Malgorzata Figiel, Miroslav Krepl, Jaroslaw Poznanski, Agnieszka Golab, Jirí Šponer, Marcin Nowotny

Open access · goldAbstract read
In one paragraph

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.4field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Interlocking activities of DNA polymerase β in the base excision repair pathway.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Structure of HIV-1 reverse transcriptase cleaving RNA in an RNA/DNA hybrid.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Malgorzata FigielLaboratory of Protein Structure, International Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland.
Miroslav KreplInstitute of Biophysics, Academy of Sciences of the Czech Republic, 612 65 Brno, Czech Republic.
Jaroslaw PoznanskiInstitute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, Poland.
Agnieszka GolabLaboratory of Protein Structure, International Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland.
Jirí ŠponerInstitute of Biophysics, Academy of Sciences of the Czech Republic, 612 65 Brno, Czech Republic.
Marcin NowotnyLaboratory of Protein Structure, International Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland.
International Institute of Molecular and Cell Biology · PLCzech Academy of Sciences · CZCzech Academy of Sciences, Institute of Biophysics · CZInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Replication of human immunodeficiency virus 1 (HIV-1) involves conversion of its single-stranded RNA genome to double-stranded DNA, which is integrated into the genome of the host. This conversion is catalyzed by reverse transcriptase (RT), which possesses DNA polymerase and RNase H domains. The available crystal structures suggest that at any given time the RNA/DNA substrate interacts with only one active site of the two domains of HIV-1 RT. Unknown is whether a simultaneous interaction of the substrate with polymerase and RNase H active sites is possible. Therefore, the mechanism of the coordination of the two activities is not fully understood. We performed molecular dynamics simulations to obtain a conformation of the complex in which the unwound RNA/DNA substrate simultaneously interacts with the polymerase and RNase H active sites. When the RNA/DNA hybrid was immobilized at the polymerase active site, RNase H cleavage occurred, experimentally verifying that the substrate can simultaneously interact with both active sites. These findings demonstrate the existence of a transient conformation of the HIV-1 RT substrate complex, which is important for modulating and coordinating the enzymatic activities of HIV-1 RT.

Indexed as

Catalytic DomainDNAHIV Reverse TranscriptaseMolecular Dynamics SimulationRibonuclease HRNADNAHIV Reverse Transcriptasereverse transcriptase, Human immunodeficiency virus 1Ribonuclease HRNA

Identifiers

PMID28108662
PMCPMC5389522
OpenAlexW2578750663

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.