A unique amino acid substitution in the outer membrane protein OmpA causes conjugation deficiency in Escherichia coli K-12.
The outer membrane protein OmpA of E. coli K-12 can serve as a receptor for phages and is required for stabilizing mating aggregates during F'-mediated conjugation. Selection for resistance to OmpA-specific phages yields mutants with alterations in the protein at four cell surface exposed sites. It is shown that conjugation deficiency can be caused by apparently only one type of amino acid substitution at one of these sites, the replacement of glycine-154 by aspartic acid. This suggests that, in contrast to binding of phages, a ligand of the donor cell recognizes only a very small area of the protein.
Ried
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G
Max-Planck-Institut für Biologie, Tübingen, FRG.
Henning
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U
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000502:physiology*; D003227:Conjugation, Genetic; D004252:DNA Mutational Analysis; D004926:Escherichia coli / Q000502:physiology*; D013329:Structure-Activity Relationship
D001425:Bacterial Outer Membrane Proteins