Outer membrane porin proteins F, P, and D1 of Pseudomonas aeruginosa and PhoE of Escherichia coli: chemical cross-linking to reveal native oligomers.
Native oligomers of three Pseudomonas aeruginosa outer membrane porin proteins and one Escherichia coli porin were demonstrated by using a chemical cross-linking technique. P. aeruginosa protein F, the major constitutive outer membrane porin, was cross-linked to dimers in outer membrane and whole-cell cross-linking experiments. Purified preparations of P. aeruginosa proteins F, D1 (glucose induced), and P (phosphate starvation induced) and E. coli protein PhoE (Ic) were also cross-linked to reveal dimers and trimers upon two-dimensional sodium dodecyl sulfate-polyacrylamide electrophoretic analysis. Cross-linking of protein F was abolished by pretreatment of the protein with sodium dodecyl sulfate, indicating that the cross-linked products were due to native associations in the outer membrane.
D000476:Alkanesulfonates; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000032:analysis*; D003432:Cross-Linking Reagents; D004926:Escherichia coli / Q000032:analysis*; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000032:analysis*; D008698:Mesylates; D018272:Porins; D011550:Pseudomonas aeruginosa / Q000032:analysis*
D000476:Alkanesulfonates; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D008565:Membrane Proteins; D008698:Mesylates; D018272:Porins; C034827:octamethylene bis(methanethiosulfonate)