Publication Type |
pre-print |
School or College |
College of Science |
Department |
Biology |
Creator |
Hughes, Kelly T. |
Other Author |
Sato, Y.; Takaya, A.; Mouslim, C.; Yamamoto, T. |
Title |
FliT selectively enhances proteolysis of FlhC Subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP |
Date |
2014-01-01 |
Description |
We previously reported that the ClpXP ATP-dependent pro-tease specifically recognizes and degrades the flagellar master transcriptional activator complex, FlhD 4C2, to negatively control flagellar biogenesis. The flagellum-related protein, FliT, isalso a negative regulator of flagellar regulon by inhibiting the binding of FlhD 4C2 to the promoter DNA. We have found a novel pathway of FliT inhibition of FlhD 4C2 activity connected to ClpXP proteolysis. An in vitro degradation assay using purified proteins shows that FliT selectively increases ClpXP proteolysis of the FlhC subunit in the FlhD 4C2 complex. FliT behaves specifically to ClpXP-dependent proteolysis of FlhC. An in vitro interaction assay detects the ternary complex of FliT-FlhD 4C2-ClpX. FliT promotes the affinity of ClpX against FlhD 4C2 complex, whereas FliT does not directly interact with ClpX. Thus, FliT interacts with the FlhC in FlhD 4C2 complex and increases the presentation of the FlhC recognition region to ClpX. The DNA-boundformofFlhD 4C2 complexisresistanttoClpXPpro-teolysis. We suggest that the role of FliT in negatively controlling the flagellar gene expression involves increasing free molecules of FlhD 4C2 sensitive to ClpXP proteolysis by inhibiting the binding to the promoter DNA as well as enhancing the selective proteolysis of FlhC subunit by ClpXP. |
Type |
Text |
Publisher |
American Soc. for Biochemistry and Molecular Biology (ASBMB) |
Volume |
289 |
Issue |
47 |
First Page |
33001 |
Last Page |
33011 |
Technical Report Number |
0 |
Language |
eng |
Bibliographic Citation |
Sato, Y., Takaya, A., Mouslim, C., Hughes, K. T., & Yamamoto, T. (2014). FliT selectively enhances proteolysis of FlhC Subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP. Journal of Biological Chemistry, 289(47), 33001-11 |
Rights Management |
(c)American Society for Biochemistry and Molecular Biology (ASBMB) http://www.asbmb.org/ |
Format Medium |
application/pdf |
Format Extent |
1,568,460 bytes |
Identifier |
uspace,19088 |
ARK |
ark:/87278/s67m3j5w |
Setname |
ir_uspace |
ID |
713375 |
Reference URL |
https://collections.lib.utah.edu/ark:/87278/s67m3j5w |