Evidence map›Paper›PMID 30122535›Full record

ArticleMolecular cell2018

Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein.

Michael R Lawson, Wen Ma, Michael J Bellecourt, Irina Artsimovitch, Andreas Martin, Robert Landick, Klaus Schulten, James M Berger

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
7.1field-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

51 citing papers in PubMed, 90 citations in OpenAlex.

  1. RfaH licenses RNA polymerase for long-range transcription.bioRxiv : the preprint server for biology · 2026
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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

8 authors at 6 institutions in 1 country.

Michael R LawsonDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.
Wen MaCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Beckman Institute for Advanced Science Technology, Urbana, IL 61801, USA; Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Michael J BellecourtDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Irina ArtsimovitchDepartment of Microbiology and The Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Andreas MartinDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA.
Robert LandickDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA; Department of Bacteriology, University of Wisconsin-Madison, Madison, WI 53706, USA.
Klaus SchultenCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Beckman Institute for Advanced Science Technology, Urbana, IL 61801, USA; Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
James M BergerDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address: jmberger@jhmi.edu.
University of Illinois Urbana-Champaign · USUniversity of Wisconsin–Madison · USHoward Hughes Medical Institute · USJohns Hopkins University · USThe Ohio State University · USUniversity of California, Berkeley · US

Funding

THE MOLECULAR BASIS OF CELL FUNCTIONT32GM007232 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BILDER, DAVID, UNAL, ELCIN · 1985 to 2022
$36.4M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
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
Univ of Calif Berkeley Chemistry-Biology Interface ProgramT32GM066698 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CHANG, CHRISTOPHER J., FRANCIS, MATTHEW B · 2004 to 2023
$7.5M
Mechanistic Studies of Replication Initiation in ProkaryotesR37GM071747 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI James M. Berger · 2017 to 2026
$4.4M
Structure/Function Studies of DNA Replication InitiationR01GM071747 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERGER, JAMES M. · 2005 to 2016
$4.0M
Minstrel HTUV Gallery 700 Automated Crystal Growth and Imaging SystemS10OD016268 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI DOUDNA, JENNIFER A · 2013 to 2013
$377k
Howard Hughes Medical InstituteNIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM067153NIGMS NIH HHS R01 GM071747NIGMS NIH HHS R37 GM071747NIGMS NIH HHS T32 GM066698NIH HHS S10 OD016268
6 · The paper itself

Abstract

NusG/Spt5 proteins are the only transcription factors utilized by all cellular organisms. In enterobacteria, NusG antagonizes the transcription termination activity of Rho, a hexameric helicase, during the synthesis of ribosomal and actively translated mRNAs. Paradoxically, NusG helps Rho act on untranslated transcripts, including non-canonical antisense RNAs and those arising from translational stress; how NusG fulfills these disparate functions is unknown. Here, we demonstrate that NusG activates Rho by assisting helicase isomerization from an open-ring, RNA-loading state to a closed-ring, catalytically active translocase. A crystal structure of closed-ring Rho in complex with NusG reveals the physical basis for this activation and further explains how Rho is excluded from translationally competent RNAs. This study demonstrates how a universally conserved transcription factor acts to modulate the activity of a ring-shaped ATPase motor and establishes how the innate sequence bias of a termination factor can be modulated to silence pervasive, aberrant transcription.

Indexed as

Bacterial ProteinsChromosomal Proteins, Non-HistoneEscherichia coliEscherichia coli ProteinsModels, MolecularPeptide Elongation FactorsProtein ConformationRho FactorRNA, BacterialTranscriptional Elongation FactorsTranscription FactorsTranscription, GeneticTranscription Termination, GeneticBacterial ProteinsChromosomal Proteins, Non-HistoneEscherichia coli ProteinsNusG protein, E coliPeptide Elongation FactorsRho FactorRNA, BacterialSPT5 transcriptional elongation factorTranscriptional Elongation FactorsTranscription FactorsATPaseNusGRhoSpt5terminationtranscriptiontranslation

Identifiers

PMID30122535
PMCPMC6151137
OpenAlexW2886020277

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.