Evidence map›Paper›PMID 21777814›Full record

ArticleMolecular cell2011

The β subunit gate loop is required for RNA polymerase modification by RfaH and NusG.

Anastasia Sevostyanova, Georgiy A Belogurov, Rachel A Mooney, Robert Landick, Irina Artsimovitch

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 109 citations in OpenAlex.

  1. RfaH licenses RNA polymerase for long-range transcription.bioRxiv : the preprint server for biology · 2026
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  4. mBio · 2025
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  17. A translational riboswitch coordinates nascent transcription-translation coupling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Review
  19. Article
  20. Article

18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Anastasia SevostyanovaDepartment of Microbiology and the RNA Group, Ohio State University, Columbus, OH 43210, USA.
Georgiy A Belogurov
Rachel A Mooney
Robert Landick
Irina Artsimovitch
The Ohio State University · USUniversity of Wisconsin–Madison · US

Funding

STRUCTURE/FUNCTION OF TRANSCRIPTION COMPLEX RNA HAIRPINSR01GM038660 · NIGMS · WASHINGTON UNIVERSITY · PI Robert Landick · 1992 to 2026
$12.2M
Mechnanism of transcript elongation control by RfaHR01GM067153 · NIGMS · OHIO STATE UNIVERSITY · PI IRINA ARTSIMOVITCH · 2003 to 2026
$8.0M
Structure/Function of Transcription Complex RNA HairpinsR37GM038660 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI LANDICK, ROBERT · 2001 to 2010
$5.5M
STRUCTURE/FUNCTION OF TRANSCRIPTION COMPLEX RNA HAIRPINSR29GM038660 · NIGMS · WASHINGTON UNIVERSITY · PI LANDICK, ROBERT · 1987 to 1991
–
NIGMS NIH HHS GM38660NIGMS NIH HHS GM67153NIGMS NIH HHS R01 GM038660NIGMS NIH HHS R01 GM067153NIGMS NIH HHS R37 GM038660
6 · The paper itself

Abstract

In all organisms, RNA polymerase (RNAP) relies on accessory factors to complete synthesis of long RNAs. These factors increase RNAP processivity by reducing pausing and termination, but their molecular mechanisms remain incompletely understood. We identify the β gate loop as an RNAP element required for antipausing activity of a bacterial virulence factor RfaH, a member of the universally conserved NusG family. Interactions with the gate loop are necessary for suppression of pausing and termination by RfaH, but are dispensable for RfaH binding to RNAP mediated by the β' clamp helices. We hypothesize that upon binding to the clamp helices and the gate loop RfaH bridges the gap across the DNA channel, stabilizing RNAP contacts with nucleic acid and disfavoring isomerization into a paused state. We show that contacts with the gate loop are also required for antipausing by NusG and propose that most NusG homologs use similar mechanisms to increase RNAP processivity.

Indexed as

Bacterial ProteinsBinding SitesDNA-Directed RNA PolymerasesEscherichia coli ProteinsModels, MolecularOperonPeptide Elongation FactorsProtein ConformationThermus thermophilusTrans-ActivatorsTranscription FactorsBacterial ProteinsDNA-Directed RNA PolymerasesEscherichia coli ProteinsNusG protein, E coliPeptide Elongation FactorsRfaH protein, E coliRNA polymerase beta subunitTrans-ActivatorsTranscription Factors

Identifiers

PMID21777814
PMCPMC3142557
OpenAlexW2009783713

What OpenQuestion holds

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LicenceTDM
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.