Evidence map›Paper›PMID 29351743›Full record

ArticleBMC microbiology2018

Phosphate signaling through alternate conformations of the PstSCAB phosphate transporter.

Ramesh K Vuppada, Colby R Hansen, Kirsta A P Strickland, Keilen M Kelly, William R McCleary

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.8field-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

41 citing papers in PubMed, 86 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Ramesh K VuppadaDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, UT, USA.
Colby R HansenDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, UT, USA.
Kirsta A P StricklandDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, UT, USA.
Keilen M KellyDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, UT, USA.
William R McClearyDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, UT, USA. bill_mccleary@byu.edu.
Brigham Young University · US

Funding

Molecular Mechanisms of Phosphate Signaling in E. coliR15GM096222 · NIGMS · BRIGHAM YOUNG UNIVERSITY · PI MCCLEARY, WILLIAM R · 2011 to 2011
$287k
NIGMS NIH HHS R15 GM096222U.S. Public Health Service R15GM96222
6 · The paper itself

Abstract

backgroundPhosphate is an essential compound for life. Escherichia coli employs a signal transduction pathway that controls the expression of genes that are required for the high-affinity acquisition of phosphate and the utilization of alternate sources of phosphorous. These genes are only expressed when environmental phosphate is limiting. The seven genes for this signaling pathway encode the two-component regulatory proteins PhoB and PhoR, as well as the high-affinity phosphate transporter PstSCAB and an auxiliary protein called PhoU. As the sensor kinase PhoR has no periplasmic sensory domain, the mechanism by which these cells sense environmental phosphate is not known. This paper explores the hypothesis that it is the alternating conformations of the PstSCAB transporter which are formed as part of the normal phosphate transport cycle that signal phosphate sufficiency or phosphate limitation.

resultsWe tested two variants of PstB that are predicted to lock the protein in either of two conformations for their signaling output. We observed that the pstBQ160K mutant, predicted to reside in an inward-facing, open conformation signaled phosphate sufficiency whereas the pstBE179Q mutant, predicted to reside in an outward-facing, closed conformation signaled phosphate starvation. Neither mutant showed phosphate transport.

conclusionsThese results support the hypothesis that the alternating conformations of the PstSCAB transporter are sensed by PhoR and PhoU. This sensory mechanism thus controls the alternate autokinase and phospho-PhoB phosphatase activities of PhoR, which ultimately control the signaling state of the response regulator PhoB.

Indexed as

Gene Expression Regulation, BacterialAlkaline PhosphataseAmino Acid SequenceBacterial ProteinsEscherichia coliEscherichia coli ProteinsGene Expression ProfilingHistidine KinaseHomeostasisMembrane Transport ProteinsMutationPhosphatesPhosphate Transport ProteinsProtein KinasesSequence AlignmentSignal TransductionAlkaline Phosphataseautophosphorylation-dependent multifunctional protein kinaseBacterial ProteinsEscherichia coli ProteinsHistidine KinaseMembrane Transport ProteinsPhoB protein, E coliPhoR protein, BacteriaPhosphatesPhosphate Transport ProteinsphoU protein, E coliProtein KinasesTranscription FactorsABC transporterHistidine kinasePhosphate homeostasisTwo-component signal transduction

Identifiers

PMID29351743
PMCPMC5775613
OpenAlexW2782065230

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LicenceCC BY
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Registered trials

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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.