Evidence map›Paper›PMID 30010831›Full record

ArticleFEMS microbiology letters2018

Energy shifts induce membrane sequestration of DraG in Rhodospirillum rubrum independent of the ammonium transporters and diazotrophic conditions.

Helen Wang, Dominik Waluk, Ray Dixon, Stefan Nordlund, Agneta Norén

Open access · hybridAbstract read
In one paragraph

Article in FEMS microbiology letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 52% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Degradation of iprodione by a novel strainFrontiers in microbiology · 2022
    Article
  2. ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021
    Review
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 2 institutions in 2 countries.

Helen WangDepartment of Medical Biochemistry and Microbiology, Uppsala Biomedicinska Centrum, Husarg.3, S-75237 Uppsala, Sweden.
Dominik WalukDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Svante Arrhenius v. 16C, Stockholm S-10691, Sweden.
Ray DixonDepartment of Molecular Microbiology, John Innes Centre, Norwich NR47 UH, UK.
Stefan NordlundDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Svante Arrhenius v. 16C, Stockholm S-10691, Sweden.
Agneta NorénDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Svante Arrhenius v. 16C, Stockholm S-10691, Sweden.
Stockholm University · SEJohn Innes Centre · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metabolic regulation of Rhodospirillum rubrum nitrogenase is mediated at the post-translational level by the enzymes DraT and DraG when subjected to changes in nitrogen or energy status. DraT is activated during switch-off, while DraG is inactivated by reversible membrane association. We confirm here that the ammonium transporter, AmtB1, rather than its paralog AmtB2, is required for ammonium induced switch-off. Amongst several substitutions at the N100 position in DraG, only N100K failed to locate to the membrane following ammonium shock, suggesting loss of interaction through charge repulsion. When switch-off was induced by lowering energy levels, either by darkness during photosynthetic growth or oxygen depletion under respiratory conditions, reversible membrane sequestration of DraG was independent of AmtB proteins and occurred even under non-diazotrophic conditions. We propose that under these conditions, changes in redox status or possibly membrane potential induce interactions between DraG and another membrane protein in response to the energy status.

Indexed as

Amino Acid MotifsAmmonium CompoundsBacterial ProteinsCell MembraneEnergy MetabolismGene Expression Regulation, BacterialMembrane Transport ProteinsN-Glycosyl HydrolasesNitrogen FixationProtein BindingRhodospirillum rubrumADP-ribosyl-(dinitrogen reductase) hydrolaseAmmonium CompoundsBacterial ProteinsMembrane Transport ProteinsN-Glycosyl HydrolasesDraGenergy switch-offmetabolic regulationnitrogenase

Identifiers

PMID30010831
PMCPMC6067124
OpenAlexW2883933651

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.