PMID:12813095: Difference between revisions

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<span style = 'font-size: large'> '''Minamino, T, González-Pedrajo, B, Kihara, M, Namba, K and Macnab, RM'''  (2003) The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH.''J. Bacteriol.'' '''185''':3983-8</span>
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!align=left  |Citation
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'''Minamino, T, González-Pedrajo, B, Kihara, M, Namba, K and Macnab, RM'''  (2003) The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH. ''J. Bacteriol.'' '''185''':3983-8
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!align=left  |Abstract
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Salmonella FliI is the ATPase that drives flagellar protein export. It normally exists as a complex together with the regulatory protein FliH. A fliH null mutant was slightly motile, with overproduction of FliI resulting in substantial improvement of its motility. Mutations in the cytoplasmic domains of FlhA and FlhB, which are integral membrane components of the type III flagellar export apparatus, also resulted in substantially improved motility, even at normal FliI levels. Thus, FliH, though undoubtedly important, is not essential.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12813095 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC161568 PMC161568]


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|{{TableHeadingColor}} |'''Abstract''' || Salmonella FliI is the ATPase that drives flagellar protein export. It normally exists as a complex together with the regulatory protein FliH. A fliH null mutant was slightly motile, with overproduction of FliI resulting in substantial improvement of its motility. Mutations in the cytoplasmic domains of FlhA and FlhB, which are integral membrane components of the type III flagellar export apparatus, also resulted in substantially improved motility, even at normal FliI levels. Thus, FliH, though undoubtedly important, is not essential.
!align=left  |Keywords
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Adenosine Triphosphatases/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Biological Transport; Flagella/metabolism; Gene Expression Regulation, Bacterial; Membrane Proteins/genetics; Membrane Proteins/metabolism; Point Mutation; Proteins/metabolism; Proton-Translocating ATPases; Salmonella/genetics; Salmonella/metabolism; Salmonella/physiology
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12813095 PubMed]
 
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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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Latest revision as of 04:20, 15 September 2013

Citation

Minamino, T, González-Pedrajo, B, Kihara, M, Namba, K and Macnab, RM (2003) The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH. J. Bacteriol. 185:3983-8

Abstract

Salmonella FliI is the ATPase that drives flagellar protein export. It normally exists as a complex together with the regulatory protein FliH. A fliH null mutant was slightly motile, with overproduction of FliI resulting in substantial improvement of its motility. Mutations in the cytoplasmic domains of FlhA and FlhB, which are integral membrane components of the type III flagellar export apparatus, also resulted in substantially improved motility, even at normal FliI levels. Thus, FliH, though undoubtedly important, is not essential.

Links

PubMed PMC161568

Keywords

Adenosine Triphosphatases/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Biological Transport; Flagella/metabolism; Gene Expression Regulation, Bacterial; Membrane Proteins/genetics; Membrane Proteins/metabolism; Point Mutation; Proteins/metabolism; Proton-Translocating ATPases; Salmonella/genetics; Salmonella/metabolism; Salmonella/physiology

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