The Escherichia coli K99 periplasmic chaperone FanE is a monomeric protein.
The monomeric or dimeric nature of the K99 periplasmic chaperone FanE was examined. The gene encoding FanE was subcloned in a pINIIIA1 derivative expression vector. A complementation experiment showed that the subcloned FanE was biologically functional. The protein was purified from the periplasm of cells harbouring the constructed plasmid. Automated Edman degradation experiments confirmed the predicted N-terminal amino acid sequence of FanE. A polyclonal mouse antiserum was raised against the FanE chaperone. The monomeric or oligomeric nature of the protein in the periplasm was studied by gel filtration, immunoblotting and chemical cross-linking experiments. The results indicated that FanE is a monomeric protein, in contrast to the K88 periplasmic chaperone.
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Department of Molecular Microbiology, BioCentrum Amsterdam, Faculty of Biology, Vrije Universiteit, The Netherlands.
Fokkema
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Oudega
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D000818:Animals; D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial / Q000737:chemistry / Q000235:genetics; D000954:Antigens, Surface / Q000737:chemistry / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D001427:Bacterial Toxins; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D051379:Mice; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D011487:Protein Conformation
D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D029968:Escherichia coli Proteins; C031429:K99 antigen; D018832:Molecular Chaperones; C070011:fanE protein, E coli