PMID:17002279
| Citation |
McMurry, JL, Murphy, JW and González-Pedrajo, B (2006) The FliN-FliH interaction mediates localization of flagellar export ATPase FliI to the C ring complex. Biochemistry 45:11790-8 |
|---|---|
| Abstract |
FliH regulates the flagellar export ATPase FliI, preventing nonproductive ATP hydrolysis. FliH has been shown to stably associate with the C ring protein FliN. Analysis of this complex reveals that FliH is required for FliI localization to the C ring, and thus FliH not only inhibits FliI ATPase activity but also may act to target FliI to the basal body. Quantitative binding studies revealed a KD of 110 nM for FliH binding to FliN. The KD for FliH binding of a FliN variant from a temperature-sensitive nonflagellate fliN point mutant was determined to be 270 nM, suggesting a molecular explanation for its phenotype. Another variant FliN from a temperature-sensitive mutant with a different phenotype displayed binding with an intermediate affinity. Weak export activity in a fliN null mutant was greatly increased by overproduction of FliI, mimicking a previously observed FliH bypass effect and supporting the conclusion that FliN-FliH binding is important for localization of FliI to the C ring and thus the membrane-embedded export apparatus beyond. A model incorporating the present findings is presented. |
| Links |
PubMed Online version:10.1021/bi0605890 |
| Keywords |
Adenosine Triphosphate/chemistry; Adenosine Triphosphate/genetics; Adenosine Triphosphate/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Membrane/chemistry; Cell Membrane/genetics; Cell Membrane/metabolism; Flagella/chemistry; Flagella/genetics; Flagella/metabolism; Hot Temperature; Multiprotein Complexes/chemistry; Multiprotein Complexes/genetics; Multiprotein Complexes/metabolism; Mutation; Protein Binding; Protein Structure, Tertiary/genetics; Protein Transport/genetics; Proton-Translocating ATPases/chemistry; Proton-Translocating ATPases/genetics; Proton-Translocating ATPases/metabolism; Salmonella enterica/chemistry; Salmonella enterica/genetics; Salmonella enterica/metabolism |
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