Evidence map›Paper›PMID 24794560›Full record

ArticleJournal of bacteriology2014

A putative bifunctional histidine kinase/phosphatase of the HWE family exerts positive and negative control on the Sinorhizobium meliloti general stress response.

Laurent Sauviac, Claude Bruand

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
7.0field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

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  7. MostmSphere · 2018
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  18. Complex two-component signaling regulates the general stress response in Alphaproteobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2014
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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

2 authors at 2 institutions in 1 country.

Laurent SauviacLaboratoire des Interactions Plantes-Microorganismes (LIPM), UMR 441 INRA, Castanet-Tolosan, France, and Laboratoire des Interactions Plantes-Microorganismes (LIPM), UMR 2594 CNRS, Castanet-Tolosan, France.
Claude BruandLaboratoire des Interactions Plantes-Microorganismes (LIPM), UMR 441 INRA, Castanet-Tolosan, France, and Laboratoire des Interactions Plantes-Microorganismes (LIPM), UMR 2594 CNRS, Castanet-Tolosan, France claude.bruand@toulouse.inra.fr.
Centre National de la Recherche Scientifique · FRLaboratoire des Interactions Plantes Micro-Organismes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The EcfG-type sigma factor RpoE2 is the regulator of the general stress response in Sinorhizobium meliloti. RpoE2 activity is negatively regulated by two NepR-type anti-sigma factors (RsiA1/A2), themselves under the control of two anti-anti-sigma factors (RsiB1/B2) belonging to the PhyR family of response regulators. The current model of RpoE2 activation suggests that in response to stress, RsiB1/B2 are activated by phosphorylation of an aspartate residue in their receiver domain. Once activated, RsiB1/B2 become able to interact with the anti-sigma factors and release RpoE2, which can then associate with the RNA polymerase to transcribe its target genes. The purpose of this work was to identify and characterize proteins involved in controlling the phosphorylation status of RsiB1/B2. Using in vivo approaches, we show that the putative histidine kinase encoded by the rsiC gene (SMc01507), located downstream from rpoE2, is able to both positively and negatively regulate the general stress response. In addition, our data suggest that the negative action of RsiC results from inhibition of RsiB1/B2 phosphorylation. From these observations, we propose that RsiC is a bifunctional histidine kinase/phosphatase responsible for RsiB1/B2 phosphorylation or dephosphorylation in the presence or absence of stress, respectively. Two proteins were previously proposed to control PhyR phosphorylation in Caulobacter crescentus and Sphingomonas sp. strain FR1. However, these proteins contain a Pfam:HisKA_2 domain of dimerization and histidine phosphotransfer, whereas S. meliloti RsiC harbors a Pfam:HWE_HK domain instead. Therefore, this is the first report of an HWE_HK-containing protein controlling the general stress response in Alphaproteobacteria.

Indexed as

Stress, PhysiologicalBacterial ProteinsGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicHistidine KinasePhosphoric Monoester HydrolasesPhosphorylationProtein KinasesSinorhizobium melilotiBacterial ProteinsHistidine KinasePhosphoric Monoester HydrolasesProtein Kinases

Identifiers

PMID24794560
PMCPMC4097584
OpenAlexW2016231502

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.