Evidence map›Paper›PMID 28811596›Full record

ArticleScientific reports2017

Complete alanine scanning of the Escherichia coli RbsB ribose binding protein reveals residues important for chemoreceptor signaling and periplasmic abundance.

Artur Reimer, Vitali Maffenbeier, Manupriyam Dubey, Vladimir Sentchilo, Diogo Tavares, Manuel Hernandez Gil, Siham Beggah, Jan Roelof van der Meer

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

7 citing papers in PubMed, 15 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

8 authors at 1 institution in 1 country.

Artur ReimerDepartment of Fundamental Microbiology, University of Lausanne, 1015, Lausanne, Switzerland.
Vitali MaffenbeierDepartment of Fundamental Microbiology, University of Lausanne, 1015, Lausanne, Switzerland.
Manupriyam DubeyDepartment of Fundamental Microbiology, University of Lausanne, 1015, Lausanne, Switzerland.
Vladimir SentchiloDepartment of Fundamental Microbiology, University of Lausanne, 1015, Lausanne, Switzerland.
Diogo TavaresDepartment of Fundamental Microbiology, University of Lausanne, 1015, Lausanne, Switzerland.
Manuel Hernandez GilDepartment of Fundamental Microbiology, University of Lausanne, 1015, Lausanne, Switzerland.
Siham BeggahDepartment of Fundamental Microbiology, University of Lausanne, 1015, Lausanne, Switzerland.
Jan Roelof van der MeerDepartment of Fundamental Microbiology, University of Lausanne, 1015, Lausanne, Switzerland. janroelof.vandermeer@unil.ch.ORCID 0000-0003-1485-3082
University of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Escherichia coli RbsB ribose binding protein has been used as a scaffold for predicting new ligand binding functions through in silico modeling, yet with limited success and reproducibility. In order to possibly improve the success of predictive modeling on RbsB, we study here the influence of individual residues on RbsB-mediated signaling in a near complete library of alanine-substituted RbsB mutants. Among a total of 232 tested mutants, we found 10 which no longer activated GFPmut2 reporter expression in E. coli from a ribose-RbsB hybrid receptor signaling chain, and 13 with significantly lower GFPmut2 induction than wild-type. Quantitative mass spectrometry abundance measurements of 25 mutants and wild-type RbsB in periplasmic space showed four categories of effects. Some (such as D89A) seem correctly produced and translocated but fail to be induced with ribose. Others (such as N190A) show lower induction probably as a result of less efficient production, folding and translocation. The third (such as N41A or K29A) have defects in both induction and abundance. The fourth category consists of semi-constitutive mutants with increased periplasmic abundance but maintenance of ribose induction. Our data show how RbsB modeling should include ligand-binding as well as folding, translocation and receptor binding.

Indexed as

Molecular ImagingSignal TransductionAlanineAmino Acid SubstitutionEscherichia coliEscherichia coli ProteinsModels, BiologicalModels, MolecularMolecular ConformationMutationPeriplasmic Binding ProteinsProtein BindingProtein TransportRiboseAlanineEscherichia coli ProteinsPeriplasmic Binding ProteinsRbsB protein, E coliRibose

Identifiers

PMID28811596
PMCPMC5557919
OpenAlexW2742564951

What OpenQuestion holds

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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.