Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex.

Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex. Research Abstract Details 

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Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex. Abstract Text:

The switch complex at the base of the bacterial flagellum is essential for flagellar assembly, rotation, and switching. In Escherichia coli and Salmonella, the complex contains about 26 copies of FliG, 34 copies of FliM, and more then 100 copies of FliN, together forming the basal body C ring. FliG is involved most directly in motor rotation and is located in the upper (membrane-proximal) part of the C ring. A crystal structure of the middle and C-terminal parts of FliG shows two globular domains connected by an alpha-helix and a short extended segment. The middle domain of FliG has a conserved surface patch formed by the residues EHPQ(125-128) and R(160) (the EHPQR motif), and the C-terminal domain has a conserved surface hydrophobic patch. To examine the functional importance of these and other surface features of FliG, we made mutations in residues distributed over the protein surface and measured the effects on flagellar assembly and function. Mutations preventing flagellar assembly occurred mainly in the vicinity of the EHPQR motif and the hydrophobic patch. Mutations causing aberrant clockwise or counterclockwise motor bias occurred in these same regions and in the waist between the upper and lower parts of the C-terminal domain. Pull-down assays with glutathione S-transferase-FliM showed that FliG interacts with FliM through both the EHPQR motif and the hydrophobic patch. We propose a model for the organization of FliG and FliM subunits that accounts for the FliG-FliM interactions identified here and for the different copy numbers of FliG and FliM in the flagellum.

Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex. Publishing Authors By Initials

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research

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Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of bacteriology

VOLUME: 189

Page Numbers: 305-12

Journal Abbreviation: J. Bacteriol.

ISSN: 0021-9193

DAY: 3

MONTH: 11

YEAR: 2006

Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985120

Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex. Keywords Mesh Terms:

KEYWORDS: Structure-Activity Relationship

MESH TERMS: metabolism

Chemical & Substance for Abstract: Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex. Information

Substance Name: FliM protein, Bacteria

Registry Number: 134548-59-7

Grant and Affiliation Information for Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex.

AFFILIATION: Department of Biology, University of Utah, Salt Lake City, UT 84112-0840, USA.

Country: United States

AGENCY: United States NIBIB

GRANT: 8R01-EB2041

ACRONYM: EB

MEDLINETA: J Bacteriol

REFSOURCE: J Bacteriol. 2007 Jan;189(2):291-3

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