Evidence map›Paper›PMID 28106310›Full record

ArticleMolecular microbiology2017

Mechanism of type-III protein secretion: Regulation of FlhA conformation by a functionally critical charged-residue cluster.

Marc Erhardt, Paige Wheatley, Eun A Kim, Takanori Hirano, Yang Zhang, Mayukh K Sarkar, Kelly T Hughes, David F Blair

Abstract read
In one paragraph

Article in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Global expression profile of enterohemorrhagic Escherichia coli O157:H7 in phagosome of murine macrophages.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026
    Article
  2. Article
  3. A β-cap on the FliPQR protein-export channel acts as the cap for initial flagellar rod assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. A biofilm-tropiceLife · 2025
    Article
  5. Bacterial motility depends on a critical flagellum length and energy-optimized assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
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  17. Article
  18. Membrane voltage-dependent activation mechanism of the bacterial flagellar protein export apparatus.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
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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.

Marc ErhardtDepartment of Biology, University of Utah, Salt Lake City, UT, 84112, USA.ORCID 0000-0001-6292-619X
Paige WheatleyDepartment of Biology, University of Utah, Salt Lake City, UT, 84112, USA.ORCID 0000-0002-5324-0089
Eun A KimDepartment of Biology, University of Utah, Salt Lake City, UT, 84112, USA.
Takanori HiranoDepartment of Biology, University of Utah, Salt Lake City, UT, 84112, USA.
Yang ZhangDepartment of Biology, University of Utah, Salt Lake City, UT, 84112, USA.
Mayukh K SarkarUniversity of Texas Medical Branch, Galveston, TX, USA.
Kelly T HughesDepartment of Biology, University of Utah, Salt Lake City, UT, 84112, USA.
David F BlairDepartment of Biology, University of Utah, Salt Lake City, UT, 84112, USA.

Funding

Coupling gene regulation to flagellar morphogenesisR01GM056141 · NIGMS · UNIVERSITY OF WASHINGTON · PI HUGHES, KELLY T · 1998 to 2023
$8.3M
Structure and Mechanism of the Flagellar Switch ComplexR01GM064664 · NIGMS · UNIVERSITY OF UTAH · PI BLAIR, DAVID F., CRANE, BRIAN R · 2003 to 2017
$4.1M
Mechanism of flagellar type-III secretionR01GM087260 · NIGMS · UNIVERSITY OF UTAH · PI BLAIR, DAVID F. · 2009 to 2010
$485k
NIGMS NIH HHS R01 GM056141NIGMS NIH HHS R01 GM064664NIGMS NIH HHS R01 GM087260
6 · The paper itself

Abstract

The bacterial flagellum contains a specialized secretion apparatus in its base that pumps certain protein subunits through the growing structure to their sites of installation beyond the membrane. A related apparatus functions in the injectisomes of gram-negative pathogens to export virulence factors into host cells. This mode of protein export is termed type-III secretion (T3S). Details of the T3S mechanism are unclear. It is energized by the proton gradient; here, a mutational approach was used to identify proton-binding groups that might function in transport. Conserved proton-binding residues in all the membrane components were tested. The results identify residues R147, R154 and D158 of FlhA as most critical. These lie in a small, well-conserved cytoplasmic domain of FlhA, located between transmembrane segments 4 and 5. Two-hybrid experiments demonstrate self-interaction of the domain, and targeted cross-linking indicates that it forms a multimeric array. A mutation that mimics protonation of the key acidic residue (D158N) was shown to trigger a global conformational change that affects the other, larger cytoplasmic domain that interacts with the export cargo. The results are discussed in the framework of a transport model based on proton-actuated movements in the cytoplasmic domains of FlhA.

Indexed as

Amino Acid SequenceBacterial ProteinsFlagellaMembrane ProteinsMutationProtein ConformationProtein Structure, TertiaryProtein TransportStructure-Activity RelationshipType III Secretion SystemsBacterial ProteinsFlhA protein, BacteriaMembrane ProteinsType III Secretion Systems

Identifiers

PMID28106310
PMCPMC5380474

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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.