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!align=left |Citation | |||
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'''Cohen-Ben-Lulu, GN, Francis, NR, Shimoni, E, Noy, D, Davidov, Y, Prasad, K, Sagi, Y, Cecchini, G, Johnstone, RM and Eisenbach, M''' (2008) The bacterial flagellar switch complex is getting more complex. ''EMBO J.'' '''27''':1134-44 | |||
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!align=left |Abstract | |||
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The mechanism of function of the bacterial flagellar switch, which determines the direction of flagellar rotation and is essential for chemotaxis, has remained an enigma for many years. Here we show that the switch complex associates with the membrane-bound respiratory protein fumarate reductase (FRD). We provide evidence that FRD binds to preparations of isolated switch complexes, forms a 1:1 complex with the switch protein FliG, and that this interaction is required for both flagellar assembly and switching the direction of flagellar rotation. We further show that fumarate, known to be a clockwise/switch factor, affects the direction of flagellar rotation through FRD. These results not only uncover a new component important for switching and flagellar assembly, but they also reveal that FRD, an enzyme known to be primarily expressed and functional under anaerobic conditions in Escherichia coli, nonetheless, has important, unexpected functions under aerobic conditions. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=18337747 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2323253 PMC2323253] | |||
Online version:[http://dx.doi.org/10.1038/emboj.2008.48 10.1038/emboj.2008.48] | |||
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!align=left |Keywords | |||
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Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli/ultrastructure; Flagella/enzymology; Flagella/metabolism; Flagella/ultrastructure; Fumarates/metabolism; Gene Deletion; Genes, Switch; Protein Binding; Recombinant Fusion Proteins/metabolism; Succinate Dehydrogenase/isolation & purification; Succinate Dehydrogenase/metabolism | |||
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==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
<annotationlinks/> | |||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
{{LitLinks}} | |||
==See also== | |||
==References== | |||
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<references/> | |||
Latest revision as of 00:48, 4 August 2015
| Citation |
Cohen-Ben-Lulu, GN, Francis, NR, Shimoni, E, Noy, D, Davidov, Y, Prasad, K, Sagi, Y, Cecchini, G, Johnstone, RM and Eisenbach, M (2008) The bacterial flagellar switch complex is getting more complex. EMBO J. 27:1134-44 |
|---|---|
| Abstract |
The mechanism of function of the bacterial flagellar switch, which determines the direction of flagellar rotation and is essential for chemotaxis, has remained an enigma for many years. Here we show that the switch complex associates with the membrane-bound respiratory protein fumarate reductase (FRD). We provide evidence that FRD binds to preparations of isolated switch complexes, forms a 1:1 complex with the switch protein FliG, and that this interaction is required for both flagellar assembly and switching the direction of flagellar rotation. We further show that fumarate, known to be a clockwise/switch factor, affects the direction of flagellar rotation through FRD. These results not only uncover a new component important for switching and flagellar assembly, but they also reveal that FRD, an enzyme known to be primarily expressed and functional under anaerobic conditions in Escherichia coli, nonetheless, has important, unexpected functions under aerobic conditions. |
| Links |
PubMed PMC2323253 Online version:10.1038/emboj.2008.48 |
| Keywords |
Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli/ultrastructure; Flagella/enzymology; Flagella/metabolism; Flagella/ultrastructure; Fumarates/metabolism; Gene Deletion; Genes, Switch; Protein Binding; Recombinant Fusion Proteins/metabolism; Succinate Dehydrogenase/isolation & purification; Succinate Dehydrogenase/metabolism |
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