Membrane association of active plasmid partitioning protein A in Escherichia coli.
QsopA and SopA, proteins essential for stable maintenance of low copy number plasmids and encoded on plasmid QpH1 of Coxiella burnetii and the F plasmid of Escherichia coli, respectively, are shown to be membrane associated using three independent approaches: isolation of hybrid protein A-PhoA proteins that display PhoA (bacterial alkaline phosphatase) activity indicating a periplasmic location, biochemical fractionation by flotation gradient centrifugation, and subcellular localization by immunoelectron microscopy. These data provide insight into the mechanism by which partitioning protein A spatially directs plasmids into daughter cells at bacterial division.
Lin
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Department of Microbiology, Washington State University, Pullman, Washington 99164, USA.
Mallavia
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LP
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism* / Q000648:ultrastructure; D005144:F Factor; D007425:Intracellular Membranes / Q000378:metabolism / Q000648:ultrastructure; D016253:Microscopy, Immunoelectron; D016296:Mutagenesis; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D013205:Staphylococcal Protein A / Q000235:genetics / Q000378:metabolism*; D015534:Trans-Activators / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; C094986:QsopA protein, Coxiella burnetii; D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A; D015534:Trans-Activators; C060971:SopA protein, Bacteria