Evidence map›Paper›PMID 33753485›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Assembly of a dsRNA synthesizing complex: RNA-DEPENDENT RNA POLYMERASE 2 contacts the largest subunit of NUCLEAR RNA POLYMERASE IV.

Vibhor Mishra, Jasleen Singh, Feng Wang, Yixiang Zhang, Akihito Fukudome, Jonathan C Trinidad, Yuichiro Takagi, Craig S Pikaard

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structure and RNA template requirements ofProceedings of the National Academy of Sciences of the United States of America · 2021
    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

8 authors.

Vibhor MishraHHMI, Indiana University, Bloomington, IN 47405.ORCID 0000-0002-4846-4790
Jasleen SinghDepartment of Biology and Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405.
Feng WangHHMI, Indiana University, Bloomington, IN 47405.ORCID 0000-0002-4760-8211
Yixiang ZhangDepartment of Chemistry, Indiana University, Bloomington, IN 47405.ORCID 0000-0003-3422-8436
Akihito FukudomeHHMI, Indiana University, Bloomington, IN 47405.
Jonathan C TrinidadDepartment of Chemistry, Indiana University, Bloomington, IN 47405.ORCID 0000-0002-8279-1509
Yuichiro TakagiDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202.ORCID 0000-0002-0988-6798
Craig S PikaardHHMI, Indiana University, Bloomington, IN 47405; cpikaard@indiana.edu.ORCID 0000-0001-8204-7459

Funding

Roles of RNA Polymerases IV and V in siRNA-mediated gene silencingR01GM077590 · NIGMS · WASHINGTON UNIVERSITY · PI PIKAARD, CRAIG STUART · 2006 to 2020
$3.5M
Mechanism of transcription regulation by the MediatorR01GM111695 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI TAKAGI, YUICHIRO · 2015 to 2019
$1.5M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM077590NIGMS NIH HHS R01 GM111695
6 · The paper itself

Abstract

In plants, transcription of selfish genetic elements such as transposons and DNA viruses is suppressed by RNA-directed DNA methylation. This process is guided by 24-nt short-interfering RNAs (siRNAs) whose double-stranded precursors are synthesized by DNA-dependent NUCLEAR RNA POLYMERASE IV (Pol IV) and RNA-DEPENDENT RNA POLYMERASE 2 (RDR2). Pol IV and RDR2 coimmunoprecipitate, and their activities are tightly coupled, yet the basis for their association is unknown. Here, we show that an interval near the RDR2 active site contacts the Pol IV catalytic subunit, NRPD1, the largest of Pol IV's 12 subunits. Contacts between the catalytic regions of the two enzymes suggests that RDR2 is positioned to rapidly engage the free 3' ends of Pol IV transcripts and convert these single-stranded transcripts into double-stranded RNAs (dsRNAs).

Indexed as

Arabidopsis ProteinsCatalytic DomainDNA-Directed RNA PolymerasesMolecular Docking SimulationMutagenesis, Site-DirectedRecombinant ProteinsRNA-Dependent RNA PolymeraseRNA, Double-StrandedTwo-Hybrid System TechniquesArabidopsis ProteinsDNA-Directed RNA PolymerasesNRPD1A protein, ArabidopsisRDR2 protein, ArabidopsisRecombinant ProteinsRNA-Dependent RNA PolymeraseRNA, Double-Strandedgene silencingPol IVRDR2RNA-directed DNA methylationRNA interference

Identifiers

PMID33753485
PMCPMC8020760

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.