Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH.

doi:10.1016/S0022-2836(02)00172-9

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Article

Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH.

Journal of molecular biology - 10 May 2002

Auvray Frédéric, Ozin Amanda J, Claret Laurent, Hughes Colin

Abstract excerpt

The specialised ATPase FliI is central to export of flagellar axial protein subunits during flagellum assembly. We establish the normal cellular location of FliI and its regulatory accessory protein FliH in motile Salmonella typhimurium, and ascertain the regions involved in FliH(2)/FliI heterotrimerisation. Both FliI and FliH localised to the cytoplasmic membrane in the presence and in the absence of proteins...

Topics

Adenosine Triphosphatases
Adenosine Triphosphate
Bacterial Proteins
Biological Transport
Cell Membrane
Cytoplasm
Dimerization
Escherichia coli Proteins
Flagella
Gene Deletion
Liposomes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Membrane Proteins

Membrane Transport Proteins

Mutation

Phospholipids

Precipitin Tests

Recombinant Proteins

SEC Translocation Channels

Source

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Identifiers

PMID: 12054792
DOI: 10.1016/S0022-2836(02)00172-9
PMCID: PMC2528292

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Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH.PMID 12054792Read ↗

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