Evidence map›Paper›PMID 28667283›Full record

ArticleScientific reports2017

The role of the FliD C-terminal domain in pentamer formation and interaction with FliT.

Hee Jung Kim, Woongjae Yoo, Kyeong Sik Jin, Sangryeol Ryu, Hyung Ho Lee

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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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.

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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

5 authors.

Hee Jung KimDepartment of Chemistry, College of Natural Sciences, Seoul National University, Seoul, 08826, Korea.
Woongjae YooDepartment of Food and Animal Biotechnology, Department of Agricultural Biotechnology, and Research Institute for Agriculture and Life Sciences, Seoul National University, Seoul, 08826, Korea.
Kyeong Sik JinPohang Accelerator Laboratory, Pohang University of Science and Technology, 80 Jigokro-127-beongil, Nam-Gu, Pohang, Kyungbuk, 37673, Korea.
Sangryeol RyuDepartment of Food and Animal Biotechnology, Department of Agricultural Biotechnology, and Research Institute for Agriculture and Life Sciences, Seoul National University, Seoul, 08826, Korea.
Hyung Ho LeeDepartment of Chemistry, College of Natural Sciences, Seoul National University, Seoul, 08826, Korea. hyungholee@snu.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flagellar biogenesis is controlled by a negative feedback loop. When FliD was secreted at the late step of flagellar assembly, the FliD-FliT complex disassembled and free FliT bound to the FlhDC complex, a master regulator of flagellar biogenesis, subsequently inhibiting the overall expression of flagellar proteins. In this study, we analyzed the role of the FliD C-terminal domain in pentamer formation and interaction with FliT. Our study showed that the FliD L443R mutant exists as a monomer in solution, indicating that the Leu443 residue of FliD, which contributes to its interaction with FliT, plays a crucial role in the pentameric oligomerization of FliD. Consistently, the increased levels of free FliT proteins caused by FliD L443R mutation had negative effects on the gene expression of flagellar synthesis and reduced the expression of flagellar proteins. The lengths of flagella in each cell were significantly reduced in L443R mutant strain, suggesting that normal flagellar biogenesis was impeded. These results suggest that the C-terminal domain of FliD plays a crucial role in the pentameric oligmerization of FliD and the binding of FliT to the C-terminal domain of FliD is critical to inhibit the premature assembly of the FliD pentamer in the cytosol.

Indexed as

Protein Interaction Domains and MotifsProtein MultimerizationAmino Acid SubstitutionBacterial ProteinsFlagellaFlagellinModels, MolecularMolecular ChaperonesMultiprotein ComplexesMutationProtein BindingProtein ConformationSalmonella typhimuriumStructure-Activity RelationshipBacterial ProteinsFlaD protein, BacteriaFlagellinfliT protein, BacteriaMolecular ChaperonesMultiprotein Complexes

Identifiers

PMID28667283
PMCPMC5493677

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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.