Evidence map›Paper›PMID 26240998›Full record

ArticleeLife2015

A putative ATPase mediates RNA transcription and capping in a dsRNA virus.

Xuekui Yu, Jiansen Jiang, Jingchen Sun, Z Hong Zhou

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.1field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. In situ structures of polymerase complex of mammalian reovirus illuminate RdRp activation and transcription regulation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Viral Capsid and Polymerase in Reoviridae.Sub-cellular biochemistry · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. In situ structures of RNA-dependent RNA polymerase inside bluetongue virus before and after uncoating.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Journal of virology · 2018
    Article
  20. Functional and evolutionary analysis of viral proteins containing a Rossmann-like fold.Protein science : a publication of the Protein Society · 2018
    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

4 authors at 2 institutions in 2 countries.

Xuekui YuDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States.
Jiansen JiangDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States.
Jingchen SunDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States.
Z Hong ZhouDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States.
University of California, Los Angeles · USCalifornia NanoSystems Institute · US

Funding

Genome Structure, Transcription and Packaging of dsRNA VirusesR01AI094386 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Z Hong ZHOU · 2012 to 2026
$6.0M
High-Resolution CryoEM Reconstruction of Large ComplexesR01GM071940 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI ZHOU, Z HONG · 2006 to 2025
$5.0M
HIGH-END CRYOEM INSTRUMENT FOR UCLA ELECTRON IMAGING CTR FOR NANOMACHINES: AIDSS10RR023057 · NCRR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ZHOU, Z HONG · 2006 to 2006
$1.6M
NCRR NIH HHS 1S10RR23057NCRR NIH HHS S10 RR023057NIAID NIH HHS AI094386NIAID NIH HHS R01 AI094386NIGMS NIH HHS GM071940NIGMS NIH HHS R01 GM071940
6 · The paper itself

Abstract

mRNA transcription in dsRNA viruses is a highly regulated process but the mechanism of this regulation is not known. Here, by nucleoside triphosphatase (NTPase) assay and comparisons of six high-resolution (2.9-3.1 Å) cryo-electron microscopy structures of cytoplasmic polyhedrosis virus with bound ligands, we show that the large sub-domain of the guanylyltransferase (GTase) domain of the turret protein (TP) also has an ATP-binding site and is likely an ATPase. S-adenosyl-L-methionine (SAM) acts as a signal and binds the methylase-2 domain of TP to induce conformational change of the viral capsid, which in turn activates the putative ATPase. ATP binding/hydrolysis leads to an enlarged capsid for efficient mRNA synthesis, an open GTase domain for His217-mediated guanylyl transfer, and an open methylase-1 domain for SAM binding and methyl transfer. Taken together, our data support a role of the putative ATPase in mediating the activation of mRNA transcription and capping within the confines of the virus.

Indexed as

Transcription, GeneticAdenosine TriphosphatasesCryoelectron MicroscopyReoviridaeRNA, Double-StrandedRNA, MessengerRNA, ViralViral ProteinsAdenosine TriphosphatasesRNA, Double-StrandedRNA, MessengerRNA, ViralViral Proteinsallosteric regulationbiochemistrybiophysicsconformational changeshistidine-mediated guanylyl transferstructural biologyviral ATPase

Identifiers

PMID26240998
PMCPMC4522710
OpenAlexW1873373704

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.