Evidence map›Paper›PMID 33384667›Full record

ArticleFrontiers in microbiology2020

A Proline-Rich Element in the Type III Secretion Protein FlhB Contributes to Flagellar Biogenesis in the Beta- and Gamma-Proteobacteria.

John C Hook, Vitan Blagotinsek, Jan Pané-Farré, Devid Mrusek, Florian Altegoer, Anita Dornes, Meike Schwan, Lukas Schier, Kai M Thormann, Gert Bange

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

Article in Frontiers in microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. An overview of the structure and function of the flagellar hook FlgE protein.World journal of microbiology & biotechnology · 2023
    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

10 authors at 2 institutions in 1 country.

John C HookDepartment of Microbiology and Molecular Biology, Justus-Liebig-Universität, Giessen, Germany.
Vitan BlagotinsekSYNMIKRO Research Center, Department of Chemistry, Philipps-University Marburg, Marburg, Germany.
Jan Pané-FarréSYNMIKRO Research Center, Department of Chemistry, Philipps-University Marburg, Marburg, Germany.
Devid MrusekSYNMIKRO Research Center, Department of Chemistry, Philipps-University Marburg, Marburg, Germany.
Florian AltegoerSYNMIKRO Research Center, Department of Chemistry, Philipps-University Marburg, Marburg, Germany.
Anita DornesSYNMIKRO Research Center, Department of Chemistry, Philipps-University Marburg, Marburg, Germany.
Meike SchwanDepartment of Microbiology and Molecular Biology, Justus-Liebig-Universität, Giessen, Germany.
Lukas SchierSYNMIKRO Research Center, Department of Chemistry, Philipps-University Marburg, Marburg, Germany.
Kai M ThormannDepartment of Microbiology and Molecular Biology, Justus-Liebig-Universität, Giessen, Germany.
Gert BangeSYNMIKRO Research Center, Department of Chemistry, Philipps-University Marburg, Marburg, Germany.
Loewe Center for Synthetic Microbiology · DEUniversity of Giessen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flagella are bacterial organelles of locomotion. Their biogenesis is highly coordinated in time and space and relies on a specialized flagellar type III secretion system (fT3SS) required for the assembly of the extracellular hook, rod, and filament parts of this complex motor device. The fT3SS protein FlhB switches secretion substrate specificity once the growing hook reaches its determined length. Here we present the crystal structure of the cytoplasmic domain of the transmembrane protein FlhB. The structure visualizes a so-far unseen proline-rich region (PRR) at the very C-terminus of the protein. Strains lacking the PRR show a decrease in flagellation as determined by hook- and filament staining, indicating a role of the PRR during assembly of the hook and filament structures. Phylogenetic analysis shows that the PRR is a primary feature of FlhB proteins of flagellated beta- and gamma-proteobacteria. Taken together, our study adds another layer of complexity and organismic diversity to the process of flagella biogenesis.

Indexed as

bacteriacrystal structurefilamentflagellumflagellum assemblyFlhBmicrobiology

Identifiers

PMID33384667
PMCPMC7771051
OpenAlexW3113207843

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.