PMID:9727020
| Citation |
Donato, GM and Kawula, TH (1998) Enhanced binding of altered H-NS protein to flagellar rotor protein FliG causes increased flagellar rotational speed and hypermotility in Escherichia coli. J. Biol. Chem. 273:24030-6 |
|---|---|
| Abstract |
H-NS is an Escherichia coli nucleoid protein known only to function as a modulator of gene expression. In this study, we found that specific single amino acid substitutions in H-NS caused an approximately 50% increase in flagellum rotational speed. In fluorescence anisotropy and chemical cross-linking assays, H-NS interacted with the flagellar torque-generating rotor protein FliG to form a complex with a Kd of 2.15 microM. Furthermore, one of the altered H-NS proteins that exhibited high speed flagellum rotation bound FliG 50% tighter than wild-type H-NS. These results demonstrate the first non-regulatory role for H-NS and provide a direct correlation between H-NS-FliG binding affinities, flagellar rotation, and motor torque generation. |
| Links | |
| Keywords |
Amino Acid Substitution; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cross-Linking Reagents; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/physiology; Escherichia coli/ultrastructure; Flagella/physiology; Flagella/ultrastructure; Fluorescence Polarization; Kinetics; Microscopy, Electron, Scanning; Models, Structural; Movement; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism |
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