Interacting Components of the Flagellar Motor ofEscherichia coliRevealed by the Two-hybrid System in Yeast

Marykwas, Donna L.; Schmidt, Susan Y.; Berg, Howard C.

doi:10.1006/jmbi.1996.0109

Cited by 81 publications

(96 citation statements)

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“…Several conclusions can be drawn from these results. First, in agreement with previous work (11,12), FliG self-associated (Fig. 4C) in the absence (reaction 3) and presence (reaction 6) of cross-linker.…”

Section: H-ns-flig Binding Via Chemicalsupporting

confidence: 92%

“…Furthermore, FliG functions primarily in flagella rotation and torque generation (12,14,15) rather than assembly or switching. Finally, there is previous genetic data indicating that fliGand hns-encoded fusion proteins interacted in a yeast twohybrid system (11).…”

Section: Discussionmentioning

confidence: 87%

“…with each other (11,12) to form a switch complex peripherally attached to the inner membrane, facing the cytoplasm (41-43). All three proteins are involved in flagellar assembly, switching, and rotation (13,14).…”

Section: Hns Mutations Cause High Speed Flagella Rotationmentioning

confidence: 99%

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Enhanced Binding of Altered H-NS Protein to Flagellar Rotor Protein FliG Causes Increased Flagellar Rotational Speed and Hypermotility in Escherichia coli

Donato

Kawula

1998

Journal of Biological Chemistry

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Section: H-ns-flig Binding Via Chemicalsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 87%

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Enhanced Binding of Altered H-NS Protein to Flagellar Rotor Protein FliG Causes Increased Flagellar Rotational Speed and Hypermotility in Escherichia coli

Donato

Kawula

1998

Journal of Biological Chemistry

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“…However, it is not known whether this high amplification reflects cooperativity of CheYϳP binding to FliM (4,25,27,28) or amplification of post-binding events at the switch (28). This question cannot be addressed by direct in vitro assays of CheY binding to purified FliM because it is not known whether purified FliM in solution truly represents the native protein within the switch complex and because the inter-FliM interactions, which normally occur within the switch (29), probably do not occur with soluble FliM molecules.…”

mentioning

confidence: 99%

Binding of the Chemotaxis Response Regulator CheY to the Isolated, Intact Switch Complex of the Bacterial Flagellar Motor

Sagi

Khan

Eisenbach

2003

Journal of Biological Chemistry

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In bacteria, the chemotactic signal is greatly amplified between the chemotaxis receptors and the flagellar motor. In Escherichia coli, part of this amplification occurs at the flagellar switch. However, it is not known whether the amplification results from cooperativity of CheY binding to the switch or from a postbinding step. To address this question, we purified the intact switch complex (constituting the switch proteins FliG, FliM, and FliN and the scaffolding protein FliF) in quantities sufficient for biochemical work and used it to investigate whether the binding of CheY to the switch complex is cooperative. As a negative control, we used complexes of switchless basal bodies, formed from the proteins FliF and FliG and similarly isolated. Using double-labeling centrifugation assays for binding, we found that CheY binds to the isolated, intact switch complex in a phosphorylation-dependent manner. We observed no significant phosphorylation-

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“…The plasmid constructs encoding those proteins were therefore omitted from further analysis. The phenomenon of self-activation, a problem that appears to affect up to 20 % of the proteins in a given genome (Nakayama et al, 2002;Uetz et al, 2000), has been observed previously for Gal4-BD fusions to the motor protein FliN of E. coli (Marykwas et al, 1996). Other motor protein fusions in that study, however, allowed assessment of their respective interactions.…”

Section: Resultsmentioning

confidence: 58%

Protein–protein interactions in the chemotaxis signalling pathway of Treponema denticola

2005

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Motile bacteria employ sophisticated chemotaxis signal transduction systems to transform environmental cues into corresponding behavioural responses. The proteins involved in this signalling pathway have been extensively studied on a molecular level in various model organisms, including enterobacteria and Bacillus subtilis, and specific protein–protein interactions have been identified. The chemotaxis operon of spirochaetes encodes a novel chemotaxis protein, CheX, in addition to homologues to the central components of established chemotaxis systems. Interestingly, the closest functionally characterized homologue of CheX is CheC of the complex B. subtilis chemotaxis pathway. In this study, the yeast two-hybrid system was applied to investigate protein–protein interactions within the chemotaxis signalling pathway of Treponema denticola, with special focus on CheX. CheX was found to interact with CheA and with itself. The other chemotaxis proteins exhibited interactions comparable to their homologues in known chemotaxis systems. Based on these findings, a model integrating CheX in the chemotaxis signal transduction pathway of T. denticola is proposed.

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Interacting Components of the Flagellar Motor ofEscherichia coliRevealed by the Two-hybrid System in Yeast

Cited by 81 publications

References 0 publications

Enhanced Binding of Altered H-NS Protein to Flagellar Rotor Protein FliG Causes Increased Flagellar Rotational Speed and Hypermotility in Escherichia coli

Enhanced Binding of Altered H-NS Protein to Flagellar Rotor Protein FliG Causes Increased Flagellar Rotational Speed and Hypermotility in Escherichia coli

Binding of the Chemotaxis Response Regulator CheY to the Isolated, Intact Switch Complex of the Bacterial Flagellar Motor

Protein–protein interactions in the chemotaxis signalling pathway of Treponema denticola

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