Outer membrane proteins of Escherichia coli K-12: Isolation of a common receptor protein for bacteriophage T6 and colicin K |
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Authors: | Paul A. Manning and Peter Reeves |
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Affiliation: | (1) Department of Microbiology and Immunology, University of Adelaide, 5000 Adelaide, S.A., Australia;(2) Present address: Max-Planck Institut für molekulare Genetik, Innestrasse 63-73, D-1000 Berlin 33 |
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Abstract: | Summary tsx mutants, resistant to T6-like bacteriophages and colicin K, of Escherichia coli K-12 lack an outer membrane protein of 26,000 molecular weight. This protein is shown to have receptor activity for both bacteriophage T6 and colicin K. The protein has been purified and its amino acid composition determined. Some tsx mutants appear to have an altered receptor protein, as indicated by their ability to plate extended host-range mutants of bacteriophage T6. These mutants are also cotransducible with proC and can be arranged in an order of increasing resistance to the host range phages, which appear to have differing degrees of ability to propagate on the tsx mutants.The tsx protein was shown to be catabolite repressible both by use of varying growth conditions and cya and crp mutants. |
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