Biochemical and immunological characterization of an R plasmid-encoded protein with properties resembling those of major cellular outer membrane proteins.
MRB, a major R222 plasmid-encoded protein previously described by us, is synthesized in large amounts in host Escherichia coli cells, where it is located principally in the outer membrane. Most of this protein is also bound to the peptidoglycan layer in a form which is trypsin resistant. Its monomeric molecular weight is about 29,000, but it is isolated from cell membranes in aggregate molecular weights of more than 100,000. These properties demonstrate a strong similarity between MRB and porins, major outer membrane proteins of host E. coli cells. They suggest that MRB may have an as-yet unidentified transport function, as do cellular outer membrane proteins with similar biochemical properties. By using antiserum specific for MRB, we demonstrated identity between MRB and the product of the traT gene, one of the surface exclusion proteins on the F plasmid. The synthesis of MRB was found to be constitutive, in contrast to other tra genes, which appear to be under more rigid regulation by the tra operon. These findings suggest that on R222 and other F-like R plasmids this protein has its own promoter.
D001426:Bacterial Proteins / Q000032:analysis / Q000235:genetics*; D002462:Cell Membrane / Q000032:analysis; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D008565:Membrane Proteins / Q000032:analysis / Q000235:genetics*; D008970:Molecular Weight; D011815:R Factors; D014357:Trypsin / Q000494:pharmacology
D001426:Bacterial Proteins; D008565:Membrane Proteins; D014357:Trypsin