Journal article
Bacterial Flagellin-Specific Chaperone FliS Interacts with Anti-Sigma Factor FlgM
Journal of bacteriology, Vol.196(6), pp.1215-1221
03/2014
Handle:
https://hdl.handle.net/2376/109917
PMCID: PMC3957722
PMID: 24415724
Abstract
Flagella are extracellular organelles that propel bacteria. Each flagellum consists of a basal body, a hook, and a filament. The major protein of the filament is flagellin. Induction of flagellin gene expression coincides with secretion of FlgM. The role of FlgM is to inhibit FliA (σ
28
), a flagellum-specific RNA polymerase responsible for flagellin transcription. To prevent premature polymerization of newly synthesized flagellin molecules, FliS, the flagellin-specific chaperone, binds flagellin and facilitates its export. In this study, the interaction between FlgM and FliS from
Salmonella enterica
serovar Typhimurium was characterized using gel shift, intrinsic tryptophan fluorescence, circular dichroism, limited proteolysis, and cross-linking. We have demonstrated that (i) FliS and FlgM interact specifically, forming a 1:1 complex, (ii) the FliS binding site on FlgM is proximal to or even overlaps the binding site for FliA, and (iii) FliA competes with FliS for FlgM binding.
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Details
- Title
- Bacterial Flagellin-Specific Chaperone FliS Interacts with Anti-Sigma Factor FlgM
- Creators
- Anna Galeva - Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, Washington, USANatalia Moroz - Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, Washington, USAYoung-Ho Yoon - Trans-Membrane Trafficking Unit, Okinawa Institute of Science and Technology, Okinawa, JapanKelly T Hughes - Department of Biology, University of Utah, Salt Lake City, Utah, USAFadel A Samatey - Trans-Membrane Trafficking Unit, Okinawa Institute of Science and Technology, Okinawa, JapanAlla S Kostyukova - Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, Washington, USA
- Publication Details
- Journal of bacteriology, Vol.196(6), pp.1215-1221
- Academic Unit
- Plant Pathology, Department of; Chemical Engineering and Bioengineering, School of
- Publisher
- American Society for Microbiology; 1752 N St., N.W., Washington, DC
- Identifiers
- 99900547297901842
- Language
- English
- Resource Type
- Journal article