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

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 express...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Hee Jung Kim, Woongjae Yoo, Kyeong Sik Jin, Sangryeol Ryu, Hyung Ho Lee
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ba860fc667ff4bb98c57e4c6cbbf6d3c
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:ba860fc667ff4bb98c57e4c6cbbf6d3c
record_format	dspace
spelling	oai:doaj.org-article:ba860fc667ff4bb98c57e4c6cbbf6d3c2021-12-02T16:08:21ZThe role of the FliD C-terminal domain in pentamer formation and interaction with FliT10.1038/s41598-017-02664-62045-2322https://doaj.org/article/ba860fc667ff4bb98c57e4c6cbbf6d3c2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02664-6https://doaj.org/toc/2045-2322Abstract 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.Hee Jung KimWoongjae YooKyeong Sik JinSangryeol RyuHyung Ho LeeNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hee Jung Kim Woongjae Yoo Kyeong Sik Jin Sangryeol Ryu Hyung Ho Lee The role of the FliD C-terminal domain in pentamer formation and interaction with FliT
description	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.
format	article
author	Hee Jung Kim Woongjae Yoo Kyeong Sik Jin Sangryeol Ryu Hyung Ho Lee
author_facet	Hee Jung Kim Woongjae Yoo Kyeong Sik Jin Sangryeol Ryu Hyung Ho Lee
author_sort	Hee Jung Kim
title	The role of the FliD C-terminal domain in pentamer formation and interaction with FliT
title_short	The role of the FliD C-terminal domain in pentamer formation and interaction with FliT
title_full	The role of the FliD C-terminal domain in pentamer formation and interaction with FliT
title_fullStr	The role of the FliD C-terminal domain in pentamer formation and interaction with FliT
title_full_unstemmed	The role of the FliD C-terminal domain in pentamer formation and interaction with FliT
title_sort	role of the flid c-terminal domain in pentamer formation and interaction with flit
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/ba860fc667ff4bb98c57e4c6cbbf6d3c
work_keys_str_mv	AT heejungkim theroleoftheflidcterminaldomaininpentamerformationandinteractionwithflit AT woongjaeyoo theroleoftheflidcterminaldomaininpentamerformationandinteractionwithflit AT kyeongsikjin theroleoftheflidcterminaldomaininpentamerformationandinteractionwithflit AT sangryeolryu theroleoftheflidcterminaldomaininpentamerformationandinteractionwithflit AT hyungholee theroleoftheflidcterminaldomaininpentamerformationandinteractionwithflit AT heejungkim roleoftheflidcterminaldomaininpentamerformationandinteractionwithflit AT woongjaeyoo roleoftheflidcterminaldomaininpentamerformationandinteractionwithflit AT kyeongsikjin roleoftheflidcterminaldomaininpentamerformationandinteractionwithflit AT sangryeolryu roleoftheflidcterminaldomaininpentamerformationandinteractionwithflit AT hyungholee roleoftheflidcterminaldomaininpentamerformationandinteractionwithflit
_version_	1718384555050663936

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

Ejemplares similares