Evidence map›Paper›PMID 29694856›Full record

ArticleBiophysical journal2018

T7 RNA Polymerase Discriminates Correct and Incorrect Nucleoside Triphosphates by Free Energy.

Shaogui Wu, Jiayang Wang, Xuemei Pu, Laicai Li, Quan Li

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Mechanism of RNA recognition by a Musashi RNA-binding protein.Current research in structural biology · 2022
    Review
  6. Strategies for Covalent Labeling of Long RNAs.Chembiochem : a European journal of chemical biology · 2021
    Review
  7. Dissecting nucleotide selectivity in viral RNA polymerases.Computational and structural biotechnology journal · 2021
    Review
  8. Article
  9. Article
  10. A Viral T7 RNA Polymerase Ratcheting Along DNA With Fidelity Control.Computational and structural biotechnology journal · 2019
    Review
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 4 institutions in 1 country.

Shaogui WuCollege of Chemistry and Materials Science, Sichuan Normal University, Chengdu, China. Electronic address: wsgchem@foxmail.com.
Jiayang WangCollege of Resources and Environment, Chengdu University of Information Technology, Chengdu, China.
Xuemei PuFaculty of Chemistry, Sichuan University, Chengdu, China.
Laicai LiCollege of Chemistry and Materials Science, Sichuan Normal University, Chengdu, China.
Quan LiCollege of Chemistry and Materials Science, Sichuan Normal University, Chengdu, China. Electronic address: liquan6688@163.com.
Sichuan Normal University · CNChengdu Normal University · CNChengdu University of Information Technology · CNSichuan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA polymerase (RNAP) is the primary machine responsible for transcription. Its ability to distinguish between correct (cognate) and incorrect (noncognate) nucleoside triphosphates (NTPs) is important for fidelity control in transcription. In this work, we investigated the substrate selection mechanism of T7 RNAP from the perspective of energetics. The dissociation free energies were determined for matched and unmatched base pairs in the preinsertion complex using the umbrella sampling method. A clear hydrogen-bond-rupture peak is observed in the potential of mean force curve for a matched base pair, whereas no such peaks are present in the position of mean force profiles for unmatched ones. The free-energy barrier could prevent correct substrates from being separated from the active site. Therefore, when NTPs diffuse into the active site, correct ones will stay for chemistry once they establish effective base pairing contacts with the template nucleotide, whereas incorrect ones will be withdrawn from the active site and rejected back to solution. This result provides an important energy evidence for the substrate selection mechanism of RNAP. Then we elucidated energetics and molecular details for correct NTP binding to the active site of the insertion complex. Our observations reveal that strong interactions act on the triphosphate of NTP to constrain its movement, whereas relatively weak interactions serve to position the base in the correct conformation. Triple interactions, hydrophobic contacts from residues M635 and Y639, base stacking from the 3' RNA terminal nucleotide, and base pairing from the template nucleotide act together to position the NTP base in a catalytically competent conformation. At last, we observed that incorrect NTPs cannot be as well-stabilized as the correct one in the active site when they are misincorporated in the insertion site. It is expected that our work can be helpful for comprehensively understanding details of this basic step in genetic transcription.

Indexed as

Adenosine TriphosphateCatalytic DomainDNA-Directed RNA PolymerasesModels, MolecularNucleotidesSubstrate SpecificityThermodynamicsViral ProteinsAdenosine Triphosphatebacteriophage T7 RNA polymeraseDNA-Directed RNA PolymerasesNucleotidesViral Proteins

Identifiers

PMID29694856
PMCPMC5937113
OpenAlexW2802045847

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.