Purification and properties of Myxococcus xanthus C-factor, an intercellular signaling protein.
C-factor, a Myxococcus xanthus protein that restores the developmental defects of a class of nonautonomous mutants resulting from mutation of the csgA gene, has been purified approximately 1000-fold from starved wild-type cells. The monomeric form of C-factor is a single polypeptide with a molecular mass of 17 kDa that can be solubilized by detergent from membrane components. Characterization by gel filtration and denaturing gel electrophoresis suggests that biologically active C-factor is a dimer composed of two 17-kDa monomers. Antibodies against a form of the M. xanthus csgA gene product overexpressed in Escherichia coli react with purified C-factor.
Kim
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Department of Biochemistry, Stanford University School of Medicine, California 94305.
Kaiser
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D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002793:Cholic Acids; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005798:Genes, Bacterial; D007700:Kinetics; D008970:Molecular Weight; D009154:Mutation; D009231:Myxococcales / Q000235:genetics / Q000254:growth & development*; D012995:Solubility; D013171:Spores, Bacterial / Q000502:physiology; D014462:Ultrafiltration
D001426:Bacterial Proteins; D002793:Cholic Acids; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate