Architecture of the outer membrane of Escherichia coli K12. IV. Relationship between outer membrane particles and aqueous pores.
The hypothesis that intramembraneous particles, observed in the outer membrane of Escherichia coli by freeze-fracture electron microscopy, are the morphological representation of aqueous pores, was tested. A mutant which is deficient in five major outer membrane proteins, b, c, d, e and the phage lambda receptor protein, contains a largely decreased number of intramembraneous particles and also shows a greatly decreased rate of uptake of several solutes. In derivatives of this strain which contain only one of these proteins in large amounts a strong decrease of the number of intramembraneous particles is observed, which is accompanied by a complete restoration of the rate of uptake of those solutes which use pores in which the protein in question is involved. The results provide strong evidence for the notion that an individual pore contains only one protein species, a property which has been found earlier for individual particles. The observed correlation between particles and equeous pores strongly supports the hypothesis that the particles are the morphological representation of pores. Implications of this hypothesis for the structure of the particles are discussed.
D000249:Adenosine Monophosphate / Q000378:metabolism; D002462:Cell Membrane / Q000648:ultrastructure; D002463:Cell Membrane Permeability; D002510:Cephalosporinase / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000648:ultrastructure*; D005614:Freeze Fracturing; D008320:Maltose / Q000378:metabolism; D008565:Membrane Proteins / Q000032:analysis; D009154:Mutation; D010316:Particle Size
D008565:Membrane Proteins; D000249:Adenosine Monophosphate; D008320:Maltose; D002510:Cephalosporinase