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

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 fl... Full description

Journal Title: Scientific reports 30 June 2017, Vol.7(1), pp.4418
Main Author: Kim, Hee Jung
Other Authors: Yoo, Woongjae , Jin, Kyeong Sik , Ryu, Sangryeol , Lee, Hyung Ho
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 2045-2322 ; PMID: 28667283 Version:1 ; DOI: 10.1038/s41598-017-02664-6
Link: http://pubmed.gov/28667283
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recordid: medline28667283
title: The role of the FliD C-terminal domain in pentamer formation and interaction with FliT
format: Article
creator:
  • Kim, Hee Jung
  • Yoo, Woongjae
  • Jin, Kyeong Sik
  • Ryu, Sangryeol
  • Lee, Hyung Ho
subjects:
  • Biology
ispartof: Scientific reports, 30 June 2017, Vol.7(1), pp.4418
description: 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...
language: eng
source:
identifier: E-ISSN: 2045-2322 ; PMID: 28667283 Version:1 ; DOI: 10.1038/s41598-017-02664-6
fulltext: fulltext
issn:
  • 20452322
  • 2045-2322
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titleThe role of the FliD C-terminal domain in pentamer formation and interaction with FliT
creatorKim, Hee Jung ; Yoo, Woongjae ; Jin, Kyeong Sik ; Ryu, Sangryeol ; Lee, Hyung Ho
ispartofScientific reports, 30 June 2017, Vol.7(1), pp.4418
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descriptionFlagellar 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...
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titleThe role of the FliD C-terminal domain in pentamer formation and interaction with FliT
descriptionFlagellar 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...
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abstractFlagellar 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...
doi10.1038/s41598-017-02664-6
pmid28667283
date2017-06-30