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Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein

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Four “pleiotropic transport” mutants of Escherichia coli B/r with decreased affinity for the uptake of most nutrients were found to lack a major outer membrane protein of 36,500 daltons (“porin”) previously shown to produce transmembrane diffusion channels in in vitro reconstitution experiments. Consequent decrease in outer membrane permeability was confirmed by measuring the transmembrane diffusion rate of 6-aminopenicillanic acid. Quantitative considerations on the porin-dependent permeability of the outer membrane show that (a) there may be very large differences in the actual rates of penetration, even among the “permeable” substances and (b) the numbers of porin molecules present in wild type cells is several orders of magnitude higher than that necessary for the uptake of rapidly diffusing substrates such as glocose from ordinary culture media. The absence of porin and the pleiotropic transport defect were always contransduced, and the mutation was mapped at 73.7 min between aroB and malT by P1 transduction. When “revertants” able to grow on low concentrations of lactose were selected, in addition to true revertants “suppressor” strains with increased amounts of non-porin membrane proteins were isolated.

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Correspondence to Hiroshi Nikaido.

Additional information

This paper corresponds to paper XVI of the series dealing with the bacterial outer membrane from the laboratory of H.N. The preceding paper in the series is Nikaido, Bavoil, and Hirota, J. Bacteriol., in press

Communicated by W. Arber

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Bavoil, P., Nikaido, H. & von Meyenburg, K. Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein. Molec. Gen. Genet. 158, 23–33 (1977).

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  • Escherichia Coli
  • Permeability
  • Lactose
  • Outer Membrane
  • Wild Type Cell