PMID:8943245: Difference between revisions

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<span style = 'font-size: large'> '''Fan, F and Macnab, RM'''  (1996) Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium.''J. Biol. Chem.'' '''271''':31981-8</span>
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!align=left  |Citation
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'''No author listed'''  (1996) Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium. ''J. Biol. Chem.'' '''271''':31981-8
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!align=left  |Abstract
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FliI is a protein needed for flagellar assembly in Salmonella typhimurium. It shows sequence similarity to the catalytic beta subunit of the F0F1-ATPase and is even more closely related to putative ATPases in Type III bacterial secretory pathways. A His-tagged version of FliI, which was fully functional in complementation tests, was purified to homogeneity. It had an ATPase activity of 0.16 s-1 at 25 degrees C and pH 7, and a Km for ATP of 0.3 mM; Mg2+ was required. The activity was not affected by inhibitors of the F-, V- or P-type ATPases, or inhibitors of the Type I or Type II bacterial secretory pathways. Mutations K188I and Y363S decreased the ATPase activity about 100-fold, increased the Km about 10-fold, blocked flagellar assembly, and were dominant. Other FliI mutations that disrupted flagellar protein export were found near the N terminus; they permitted essentially wild-type ATPase activity, were not dominant, and showed a dosage-dependent phenotype. We propose that FliI has a C-terminal ATPase domain and an N-terminal domain that interacts with other components in the flagellum-specific export apparatus.
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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=8943245 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || FliI is a protein needed for flagellar assembly in Salmonella typhimurium. It shows sequence similarity to the catalytic beta subunit of the F0F1-ATPase and is even more closely related to putative ATPases in Type III bacterial secretory pathways. A His-tagged version of FliI, which was fully functional in complementation tests, was purified to homogeneity. It had an ATPase activity of 0.16 s-1 at 25 degrees C and pH 7, and a Km for ATP of 0.3 mM; Mg2+ was required. The activity was not affected by inhibitors of the F-, V- or P-type ATPases, or inhibitors of the Type I or Type II bacterial secretory pathways. Mutations K188I and Y363S decreased the ATPase activity about 100-fold, increased the Km about 10-fold, blocked flagellar assembly, and were dominant. Other FliI mutations that disrupted flagellar protein export were found near the N terminus; they permitted essentially wild-type ATPase activity, were not dominant, and showed a dosage-dependent phenotype. We propose that FliI has a C-terminal ATPase domain and an N-terminal domain that interacts with other components in the flagellum-specific export apparatus.
!align=left  |Keywords
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Adenosine Diphosphate/metabolism; Adenosine Triphosphatases/metabolism; Bacterial Proteins; Chromatography, High Pressure Liquid; Electrophoresis, Polyacrylamide Gel; Genetic Complementation Test; Mutagenesis, Site-Directed; Proteins/chemistry; Proton-Translocating ATPases; Rosaniline Dyes; Salmonella typhimurium; Temperature
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8943245 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}

Revision as of 19:53, 1 September 2013

Citation

No author listed (1996) Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium. J. Biol. Chem. 271:31981-8

Abstract

FliI is a protein needed for flagellar assembly in Salmonella typhimurium. It shows sequence similarity to the catalytic beta subunit of the F0F1-ATPase and is even more closely related to putative ATPases in Type III bacterial secretory pathways. A His-tagged version of FliI, which was fully functional in complementation tests, was purified to homogeneity. It had an ATPase activity of 0.16 s-1 at 25 degrees C and pH 7, and a Km for ATP of 0.3 mM; Mg2+ was required. The activity was not affected by inhibitors of the F-, V- or P-type ATPases, or inhibitors of the Type I or Type II bacterial secretory pathways. Mutations K188I and Y363S decreased the ATPase activity about 100-fold, increased the Km about 10-fold, blocked flagellar assembly, and were dominant. Other FliI mutations that disrupted flagellar protein export were found near the N terminus; they permitted essentially wild-type ATPase activity, were not dominant, and showed a dosage-dependent phenotype. We propose that FliI has a C-terminal ATPase domain and an N-terminal domain that interacts with other components in the flagellum-specific export apparatus.

Links

PubMed

Keywords

Adenosine Diphosphate/metabolism; Adenosine Triphosphatases/metabolism; Bacterial Proteins; Chromatography, High Pressure Liquid; Electrophoresis, Polyacrylamide Gel; Genetic Complementation Test; Mutagenesis, Site-Directed; Proteins/chemistry; Proton-Translocating ATPases; Rosaniline Dyes; Salmonella typhimurium; Temperature

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