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

Collection with item attached
2017
Item details URL
http://open-repository.kisti.re.kr/cube/handle/open_repository/486109.do
DOI
10.1038/s41598-017-02664-6
Title
The role of the FliD C-terminal domain in pentamer formation andinteraction with FliT
Description
The authors thank the staff of beamline 5C at the Pohang Light Sourcefor their assistance during X-ray experiments. This study was supportedby a grant from the National Research Foundation (NRF) of Korea fundedby the Korean government (2015R1A5A1008958 and 2015R1C1A1A01054842), agrant from the Korea CCS R&D Center (KCRC; 2014M1A8A1049296), and agrant from Institute for Basic Science (IBS-R021-D1) to H. H. L. Thisstudy was also supported by a grant (14162MFDS972) from the Ministry ofFood and Drug Safety, Korea in 2016 to S. R.
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.
provenance
Made available in Cube on 2018-09-28T15:58:46Z (GMT). No. of bitstreams: 0
language
English
author
Kim, Hee Jung
Yoo, Woongjae
Jin, Kyeong Sik
Ryu, Sangryeol
Lee, Hyung Ho
accessioned
2018-09-28T15:58:46Z
available
2018-09-28T15:58:46Z
issued
2017
citation
SCIENTIFIC REPORTS(7)
issn
2045-2322
uri
http://open-repository.kisti.re.kr/cube/handle/open_repository/486109.do
Funder
교육부
Funding Program
BK21플러스사업(0.5)
Project ID
1345274045
Jurisdiction
Rep.of Korea
Project Name
Department of Agricultural Biotechnology
rights
openAccess
type
article


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