PMID:8943245: Difference between revisions
Edited by wikibot |
imported>Wikientrybot change PMID template to TableEdit version |
||
| (5 intermediate revisions by 2 users not shown) | |||
| Line 1: | Line 1: | ||
{{RightTOC}} | {{RightTOC}} | ||
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.59502.B52239b49a835a--> | |||
<!-- | |||
****************************************************************************************** | |||
* | |||
* ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | |||
* | |||
****************************************************************************************** --> | |||
{| id="B52239b49a835a" class=" tableEdit PMID_info_table" | |||
|- | |||
!align=left |Citation | |||
|| | |||
'''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 | |||
|- | |||
!align=left |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 |Links | |||
|| | |||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8943245 PubMed] | |||
|- | |- | ||
| | !align=left |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 | ||
|{{ | |||
|- class="tableEdit_footer" | |||
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.59502.B52239b49a835a&page=59502&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> || | |||
|} | |} | ||
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.59502.B52239b49a835a--> | |||
==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
| Line 18: | Line 38: | ||
==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
< | <annotationlinks/> | ||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:56, 15 September 2013
| Citation |
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 |
|---|---|
| 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 | |
| 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 |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.