Evidence map›Paper›PMID 25071209›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Single-molecule FRET reveals a corkscrew RNA structure for the polymerase-bound influenza virus promoter.

Alexandra I Tomescu, Nicole C Robb, Narin Hengrung, Ervin Fodor, Achillefs N Kapanidis

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 57 citations in OpenAlex.

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  13. Selective Genome Packaging Mechanisms of Influenza A Viruses.Cold Spring Harbor perspectives in medicine · 2021
    Review
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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

5 authors at 1 institution in 1 country.

Alexandra I TomescuBiological Physics Research Group, Clarendon Laboratory, Department of Physics, University of Oxford, Oxford OX1 3PU, United Kingdom;
Nicole C RobbBiological Physics Research Group, Clarendon Laboratory, Department of Physics, University of Oxford, Oxford OX1 3PU, United Kingdom;
Narin HengrungSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom; andDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom.
Ervin FodorSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom; and a.kapanidis1@physics.ox.ac.uk ervin.fodor@path.ox.ac.uk.
Achillefs N KapanidisBiological Physics Research Group, Clarendon Laboratory, Department of Physics, University of Oxford, Oxford OX1 3PU, United Kingdom; a.kapanidis1@physics.ox.ac.uk ervin.fodor@path.ox.ac.uk.
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J001694/1Biotechnology and Biological Sciences Research Council DKRVYA0/AKMedical Research Council G0700848Medical Research Council MR/K000241/1Wellcome Trust 092931/Z/10/Z
6 · The paper itself

Abstract

The influenza virus is a major human and animal pathogen responsible for seasonal epidemics and occasional pandemics. The genome of the influenza A virus comprises eight segments of single-stranded, negative-sense RNA with highly conserved 5' and 3' termini. These termini interact to form a double-stranded promoter structure that is recognized and bound by the viral RNA-dependent RNA polymerase (RNAP); however, no 3D structural information for the influenza polymerase-bound promoter exists. Functional studies have led to the proposal of several 2D models for the secondary structure of the bound promoter, including a corkscrew model in which the 5' and 3' termini form short hairpins. We have taken advantage of an insect-cell system to prepare large amounts of active recombinant influenza virus RNAP, and used this to develop a highly sensitive single-molecule FRET assay to measure distances between fluorescent dyes located on the promoter and map its structure both with and without the polymerase bound. These advances enabled the direct analysis of the influenza promoter structure in complex with the viral RNAP, and provided 3D structural information that is in agreement with the corkscrew model for the influenza virus promoter RNA. Our data provide insights into the mechanisms of promoter binding by the influenza RNAP and have implications for the understanding of the regulatory mechanisms involved in the transcription of viral genes and replication of the viral RNA genome. In addition, the simplicity of this system should translate readily to the study of any virus polymerase-promoter interaction.

Indexed as

Promoter Regions, GeneticAnimalsBinding SitesFluorescence Resonance Energy TransferHumansInfluenza A Virus, H3N2 SubtypeModels, MolecularNucleic Acid ConformationRNA-Dependent RNA PolymeraseRNA, ViralViral ProteinsRNA-Dependent RNA PolymeraseRNA, ViralViral Proteins

Identifiers

PMID25071209
PMCPMC4136606
OpenAlexW2031063366

What OpenQuestion holds

Textmetadata
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.