Characterization of ompF domains involved in Escherichia coli K-12 sensitivity to colicins A and N.
Various ompF-ompC, ompC-ompF, and ompF-ompC-ompF chimeric genes were used to locate the domains of the OmpF protein involved in cellular sensitivity to colicins. Various parts of the porin participate in the entry of colicins. Colicin N receptor activity was found to require three regions: RN1, located between residues 1 and 63; RN2, located between residues 115 and 262; and RN3, located between residues 279 and 297. The central domain from residues 143 to 262 is involved during the translocation step after the binding step. A large region, including residues 1 to 262, is necessary during colicin A entry. The locations and interactions between these domains specifically required for the uptake of colicins to occur are described and discussed with regard to the homology and topology of the OmpC, OmpF, and PhoE porins.
Centre de Biochimie et de Biologie Moléculaire, Centre National de la Recherche Scientifique, Marseille, France.
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Fourel
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Hikita
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Bolla
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Mizushima
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Pagès
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics*; D001665:Binding Sites; D002678:Chimera; D003087:Colicins / Q000378:metabolism / Q000494:pharmacology*; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics* / Q000254:growth & development; D005798:Genes, Bacterial; D008969:Molecular Sequence Data
D001425:Bacterial Outer Membrane Proteins; D003087:Colicins