Evidence map›Paper›PMID 28974721›Full record

ArticleScientific reports2017

Impact of fluorescent protein fusions on the bacterial flagellar motor.

M Heo, A L Nord, D Chamousset, E van Rijn, H J E Beaumont, F Pedaci

Abstract read
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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Torque-generating units of the bacterial flagellar motor are rotary motors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  14. Review
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  16. Review
  17. Catch bond drives stator mechanosensitivity in the bacterial flagellar motor.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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.

M HeoSingle-molecule Biophysics dept, Centre de Biochimie Stucturale, CNRS UMR5048 UM INSERM U1054, 29 Rue de Navacelles, 34090, Montpellier, France.
A L NordSingle-molecule Biophysics dept, Centre de Biochimie Stucturale, CNRS UMR5048 UM INSERM U1054, 29 Rue de Navacelles, 34090, Montpellier, France.
D ChamoussetSingle-molecule Biophysics dept, Centre de Biochimie Stucturale, CNRS UMR5048 UM INSERM U1054, 29 Rue de Navacelles, 34090, Montpellier, France.
E van RijnDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, 2628 CJ, Delft, The Netherlands.
H J E BeaumontDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, 2628 CJ, Delft, The Netherlands.
F PedaciSingle-molecule Biophysics dept, Centre de Biochimie Stucturale, CNRS UMR5048 UM INSERM U1054, 29 Rue de Navacelles, 34090, Montpellier, France. francesco.pedaci@cbs.cnrs.fr.ORCID 0000-0002-4530-3027

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescent fusion proteins open a direct and unique window onto protein function. However, they also introduce the risk of perturbation of the function of the native protein. Successful applications of fluorescent fusions therefore rely on a careful assessment and minimization of the side effects, but such insight is still lacking for many applications. This is particularly relevant in the study of the internal dynamics of motor proteins, where both the chemical and mechanical reaction coordinates can be affected. Fluorescent proteins fused to the stator of the Bacterial Flagellar Motor (BFM) have previously been used to unveil the motor subunit dynamics. Here we report the effects on single motors of three fluorescent proteins fused to the stators, all of which altered BFM behavior. The torque generated by individual stators was reduced while their stoichiometry remained unaffected. MotB fusions decreased the switching frequency and induced a novel bias-dependent asymmetry in the speed in the two directions. These effects could be mitigated by inserting a linker at the fusion point. These findings provide a quantitative account of the effects of fluorescent fusions to the stator on BFM dynamics and their alleviation- new insights that advance the use of fluorescent fusions to probe the dynamics of protein complexes.

Indexed as

Bacterial ProteinsEscherichia coliFlagellaMolecular Motor ProteinsMultiprotein ComplexesBacterial ProteinsMolecular Motor ProteinsMotB protein, BacteriaMultiprotein Complexes

Identifiers

PMID28974721
PMCPMC5626733

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.