Evidence map›Paper›PMID 31940802›Full record

ArticleBiomolecules2020

In Vitro Autonomous Construction of the Flagellar Axial Structure in Inverted Membrane Vesicles.

Hiroyuki Terashima, Chinatsu Tatsumi, Akihiro Kawamoto, Keiichi Namba, Tohru Minamino, Katsumi Imada

Abstract read
In one paragraph

Article in Biomolecules, 2020. 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
–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

7 citing papers in PubMed.

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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

6 authors.

Hiroyuki TerashimaDivision of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-Ku, Nagoya 464-8602, Japan.
Chinatsu TatsumiDepartment of Macromolecular Science, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
Akihiro KawamotoGraduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-7380-0127
Keiichi NambaGraduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.ORCID 0000-0003-2911-5875
Tohru MinaminoGraduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.
Katsumi ImadaDepartment of Macromolecular Science, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.ORCID 0000-0003-1342-8885

Funding

Japan Agency for Medical Research and Development JP19am0101117Japan Society for the Promotion of Science JP15H02386Japan Society for the Promotion of Science JP18K07108Japan Society for the Promotion of Science JP19H03182Japan Society for the Promotion of Science JP21227006Japan Society for the Promotion of Science JP25000013Japan Society for the Promotion of Science JP26293097Ministry of Education, Culture, Sports, Science and Technology JP15H01640Ministry of Education, Culture, Sports, Science and Technology JP23115008
6 · The paper itself

Abstract

The bacterial flagellum is a filamentous organelle extending from the cell surface. The axial structure of the flagellum consists of the rod, hook, junction, filament, and cap. The axial structure is formed by axial component proteins exported via a specific protein export apparatus in a well-regulated manner. Although previous studies have revealed the outline of the flagellar construction process, the mechanism of axial structure formation, including axial protein export, is still obscure due to difficulties in direct observation of protein export and assembly in vivo. We recently developed an in vitro flagellar protein transport assay system using inverted membrane vesicles (IMVs) and succeeded in reproducing the early stage of flagellar assembly. However, the late stage of the flagellar formation process remained to be examined in the IMVs. In this study, we showed that the filament-type proteins are transported into the IMVs to produce the filament on the hook inside the IMVs. Furthermore, we provide direct evidence that coordinated flagellar protein export and assembly can occur at the post-translational level. These results indicate that the ordered construction of the entire flagellar structure can be regulated by only the interactions between the protein export apparatus, the export substrate proteins, and their cognate chaperones.

Indexed as

Bacterial ProteinsFlagellaHumansMembrane ProteinsProtein TransportSalmonella InfectionsSalmonella typhimuriumType III Secretion SystemsBacterial ProteinsFlgD protein, Salmonella typhimuriumFlgE protein, BacteriaFlgK protein, BacteriafliH protein, BacteriaFliL protein, BacteriaMembrane ProteinsType III Secretion Systemsbacterial flagellumflagellar filamentflagellar specific export apparatusinverted membrane vesiclein vitro reconstitutionSalmonella typhimuriumtype III secretion system

Identifiers

PMID31940802
PMCPMC7022808

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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.