Evidence map›Paper›PMID 31412261›Full record

ArticleJournal of molecular biology2019

A Mechanism of Modulating the Direction of Flagellar Rotation in Bacteria by Fumarate and Fumarate Reductase.

Anna Koganitsky, Dmitry Tworowski, Tali Dadosh, Gary Cecchini, Michael Eisenbach

Abstract read
In one paragraph

Article in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
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  6. Review
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  8. 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.

Anna KoganitskyDepartment of Biomolecular Sciences, The Weizmann Institute of Science, 7610001 Rehovot, Israel.
Dmitry TworowskiDepartment of Structural Biology, The Weizmann Institute of Science, 7610001 Rehovot, Israel.
Tali DadoshDepartment of Chemical Research Support, The Weizmann Institute of Science, 7610001 Rehovot, Israel.
Gary CecchiniMolecular Biology Division, San Francisco VA Health Care System, San Francisco, CA 94121, USA; Department of Biochemistry & Biophysics, University of California, San Francisco, CA 94158, USA.
Michael EisenbachDepartment of Biomolecular Sciences, The Weizmann Institute of Science, 7610001 Rehovot, Israel. Electronic address: m.eisenbach@weizmann.ac.il.

Funding

Structure/Function of Complex ll OxidoreductasesR01GM061606 · NIGMS · NORTHERN CALIFORNIA INSTITUTE RES &EDUC · PI CECCHINI, GARY, IVERSON, T M · 2001 to 2022
$9.1M
BLR&D Research Career Scientist Award ApplicationIK6BX004215 · VA · VETERANS AFFAIRS MED CTR SAN FRANCISCO · PI CECCHINI, GARY · 2018 to 2024
–
BLRD VA IK6 BX004215NIGMS NIH HHS R01 GM061606
6 · The paper itself

Abstract

Fumarate, an electron acceptor in anaerobic respiration of Escherichia coli, has an additional function of assisting the flagellar motor to shift from counterclockwise to clockwise rotation, with a consequent modulation of the bacterial swimming behavior. Fumarate transmits its effect to the motor via the fumarate reductase complex (FrdABCD), shown to bind to FliG-one of the motor's switch proteins. How binding of the FrdABCD respiratory enzyme to FliG enhances clockwise rotation and how fumarate is involved in this activity have remained puzzling. Here we show that the FrdA subunit in the presence of fumarate is sufficient for binding to FliG and for clockwise enhancement. We further demonstrate by in vitro binding assays and super-resolution microscopy in vivo that the mechanism by which fumarate-occupied FrdA enhances clockwise rotation involves its preferential binding to the clockwise state of FliG (FliG

Indexed as

RotationAnaerobiosisAnimalsBacteriaBacterial ProteinsCattleFlagellaFluorescent DyesFumaratesMolecular Dynamics SimulationProtein BindingSuccinate DehydrogenaseBacterial ProteinsFluorescent Dyesfumarate reductase complexFumaratesSuccinate Dehydrogenaseanaerobic complex IIflagellar motorFliGprotein electrostaticsrespiratory complexes

Identifiers

PMID31412261
PMCPMC6733631

What OpenQuestion holds

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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.