PMID:15170399: Difference between revisions
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| | !align=left |Citation | ||
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'''Minamino, T and Namba, K''' (2004) Self-assembly and type III protein export of the bacterial flagellum. ''J. Mol. Microbiol. Biotechnol.'' '''7''':5-17 | |||
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!align=left |Abstract | |||
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The bacterial flagellum is a supramolecular structure consisting of a basal body, a hook and a filament. Most of the flagellar components are translocated across the cytoplasmic membrane by the flagellar type III protein export apparatus in the vicinity of the flagellar base, diffuse down the narrow channel through the nascent structure and self-assemble at its distal end with the help of a cap structure. Flagellar proteins synthesized in the cytoplasm are targeted to the export apparatus with the help of flagellum-specific chaperones and pushed into the channel by an ATPase, whose activity is controlled by its regulator to enable the energy of ATP hydrolysis to be efficiently coupled to the translocation reaction. The export apparatus switches its substrate specificity by monitoring the state of flagellar assembly in the cell exterior, allowing this huge and complex macromolecular assembly to be built efficiently by a highly ordered and well-regulated assembly process. | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15170399 PubMed] | |||
Online version:[http://dx.doi.org/10.1159/000077865 10.1159/000077865] | |||
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|{{ | !align=left |Keywords | ||
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Bacterial Proteins/metabolism; Cytoplasm/physiology; Escherichia coli/physiology; Flagella/physiology; Movement; Protein Transport; Proton-Translocating ATPases/metabolism; Salmonella/physiology; Salmonella/ultrastructure; Substrate Specificity | |||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
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==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:24, 15 September 2013
| Citation |
Minamino, T and Namba, K (2004) Self-assembly and type III protein export of the bacterial flagellum. J. Mol. Microbiol. Biotechnol. 7:5-17 |
|---|---|
| Abstract |
The bacterial flagellum is a supramolecular structure consisting of a basal body, a hook and a filament. Most of the flagellar components are translocated across the cytoplasmic membrane by the flagellar type III protein export apparatus in the vicinity of the flagellar base, diffuse down the narrow channel through the nascent structure and self-assemble at its distal end with the help of a cap structure. Flagellar proteins synthesized in the cytoplasm are targeted to the export apparatus with the help of flagellum-specific chaperones and pushed into the channel by an ATPase, whose activity is controlled by its regulator to enable the energy of ATP hydrolysis to be efficiently coupled to the translocation reaction. The export apparatus switches its substrate specificity by monitoring the state of flagellar assembly in the cell exterior, allowing this huge and complex macromolecular assembly to be built efficiently by a highly ordered and well-regulated assembly process. |
| Links |
PubMed Online version:10.1159/000077865 |
| Keywords |
Bacterial Proteins/metabolism; Cytoplasm/physiology; Escherichia coli/physiology; Flagella/physiology; Movement; Protein Transport; Proton-Translocating ATPases/metabolism; Salmonella/physiology; Salmonella/ultrastructure; Substrate Specificity |
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