Evidence map›Paper›PMID 25799498›Full record

ArticlePloS one2015

pH dependence of the stress regulator DksA.

Ran Furman, Eric M Danhart, Monali NandyMazumdar, Chunhua Yuan, Mark P Foster, Irina Artsimovitch

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

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  16. Puzzling conformational changes affecting proteins binding to the RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2018
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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

6 authors at 1 institution in 1 country.

Ran FurmanDepartment of Microbiology, The Ohio State University, Columbus, Ohio, United States of America; The Center for RNA Biology, The Ohio State University, Columbus, Ohio, United States of America.
Eric M DanhartThe Center for RNA Biology, The Ohio State University, Columbus, Ohio, United States of America; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, United States of America.
Monali NandyMazumdarDepartment of Microbiology, The Ohio State University, Columbus, Ohio, United States of America; The Center for RNA Biology, The Ohio State University, Columbus, Ohio, United States of America.
Chunhua YuanCampus Chemical Instrument Center, The Ohio State University, Columbus, Ohio, United States of America.
Mark P FosterThe Center for RNA Biology, The Ohio State University, Columbus, Ohio, United States of America; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, United States of America.
Irina ArtsimovitchDepartment of Microbiology, The Ohio State University, Columbus, Ohio, United States of America; The Center for RNA Biology, The Ohio State University, Columbus, Ohio, United States of America.
The Ohio State University · US

Funding

Mechnanism of transcript elongation control by RfaHR01GM067153 · NIGMS · OHIO STATE UNIVERSITY · PI IRINA ARTSIMOVITCH · 2003 to 2026
$8.0M
CHEMISTRY/BIOLOGY TRAINING GRANTT32GM008512 · NIGMS · OHIO STATE UNIVERSITY · PI PEI, DEHUA · 1996 to 2016
$3.9M
Structural and Dynamics in Allosteric Gene RegulationR01GM077234 · NIGMS · OHIO STATE UNIVERSITY · PI FOSTER, MARK P. · 2007 to 2010
$1.2M
NIGMS NIH HHS 3T32GM008512-14S1NIGMS NIH HHS R01 GM067153NIGMS NIH HHS R01 GM077234NIGMS NIH HHS R01 GM67153NIGMS NIH HHS T32 GM008512
6 · The paper itself

Abstract

DksA controls transcription of genes associated with diverse stress responses, such as amino acid and carbon starvation, oxidative stress, and iron starvation. DksA binds within the secondary channel of RNA polymerase, extending its long coiled-coil domain towards the active site. The cellular expression of DksA remains constant due to a negative feedback autoregulation, raising the question of whether DksA activity is directly modulated during stress. Here, we show that Escherichia coli DksA is essential for survival in acidic conditions and that, while its cellular levels do not change significantly, DksA activity and binding to RNA polymerase are increased at lower pH, with a concomitant decrease in its stability. NMR data reveal pH-dependent structural changes centered at the interface of the N and C-terminal regions of DksA. Consistently, we show that a partial deletion of the N-terminal region and substitutions of a histidine 39 residue at the domain interface abolish pH sensitivity in vitro. Together, these data suggest that DksA responds to changes in pH by shifting between alternate conformations, in which competing interactions between the N- and C-terminal regions modify the protein activity.

Indexed as

Stress, PhysiologicalDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsHistidineHydrogen-Ion ConcentrationModels, MolecularProtein ConformationProtein StabilitydksA protein, E coliDNA-Directed RNA PolymerasesEscherichia coli ProteinsHistidine

Identifiers

PMID25799498
PMCPMC4370453
OpenAlexW2115550420

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.