Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers

Penelope I. Higgs, Paul S. Myers, Kathleen Postle

Research output: Contribution to journalArticle

104 Scopus citations

Abstract

The cytoplasmic membrane proteins ExbB and ExbD support TonB-dependent active transport of iron siderophores and vitamin B12 across the essentially unenergized outer membrane of Escherichia coli. In this study, in vivo formaldehyde cross-linking analysis was used to investigate the interactions of T7 epitope-tagged ExbB or ExbD proteins. ExbB and ExbD each formed two unique cross-linked complexes which were not dependent on the presence of TonB, the outer membrane receptor protein FepA, or the other Exb protein. Cross-linking analysis of ExbB- and ExbD-derived size variants demonstrated instead that these ExbB and ExbD complexes were homodimers and homotrimers and suggested that ExbB also interacted with an unidentified protein(s). Cross-linking analysis of epitope-tagged ExbB and ExbD proteins with TonB antisera afforded detection of a previously unrecognized TonB-ExbD cross-linked complex and confirmed the composition of the TonB-ExbB cross- linked complex. The implications of these findings for the mechanism of TonB- dependent energy transduction are discussed.

Original languageEnglish (US)
Pages (from-to)6031-6038
Number of pages8
JournalJournal of bacteriology
Volume180
Issue number22
DOIs
StatePublished - Nov 1998

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

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