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A unique amino acid substitution in the outer membrane protein OmpA causes conjugation deficiency in Escherichia coli K‐12
Author(s) -
Ried Georg,
Henning Ulf
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80324-1
Subject(s) - escherichia coli , aspartic acid , bacterial outer membrane , amino acid , mutant , ligand (biochemistry) , biochemistry , biology , glycine , cell membrane , chemistry , receptor , membrane , gene
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.