Outer membrane porin proteins F, P, and D1 of Pseudomonas aeruginosa and PhoE of Escherichia coli: Chemical cross-linking to reveal native oligomers

B. L. Angus, Robert Hancock

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1042-1051
Number of pages10
JournalJournal of bacteriology
Volume155
Issue number3
Publication statusPublished - 1 Jan 1983
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this