Characterization of the receptor and translocator domains of colicin N.
Intact colicin N and various colicin derivatives, including a natural fragment lacking the first 36 amino-acid residues, a chymotryptic fragment lacking the first 66 amino acids and a thermolytic fragment comprising residues 183-387, were used to locate the regions involved in colicin-N uptake by sensitive Escherichia coli cells. Two separate domains of the molecule participate in colicin-N entry. Specific binding to OmpF receptor site requires a region located between residues 67-182. A N-terminal domain, located between residues 17-66, is involved during the translocation step after binding to receptor. Two sub-regions, residues 17-36 and residues 37-36, can be defined in this domain. The location and interactions between these domains are discussed in comparison to other colicins which use similar cell components for their uptake.
el Kouhen
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UPR9027, GDR1000 du Centre National de la Recherche Scientifique Marseille, France.
Fierobe
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HP
Scianimanico
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Steiert
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Pattus
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Pagès
J M
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D001667:Binding, Competitive; D001692:Biological Transport; D003087:Colicins / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D010446:Peptide Fragments / Q000378:metabolism*; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic / Q000378:metabolism*; D013329:Structure-Activity Relationship
D003087:Colicins; D029968:Escherichia coli Proteins; D010446:Peptide Fragments; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; C028593:colicin receptor, E coli