Biogenesis of a putative channel protein, ComEC, required for DNA uptake: Membrane topology, oligomerization and formation of disulphide bonds

Irena Draskovic, David Dubnau

Research output: Contribution to journalArticlepeer-review

110 Scopus citations

Abstract

ComEC is a putative channel protein for DNA uptake in Bacillus subtilis and other genetically transformable bacteria. Membrane topology studies suggest a model of ComEC as a multispanning membrane protein with seven transmembrane segments (TMSs), and possibly with one laterally inserted amphipathic helix. We show that ComEC contains an intramolecular disulphide bond in its N-terminal extracellular loop (between the residues C131 and C172), which is required for the stability of the protein, and is probably introduced by BdbDC, a pair of competence-induced oxidoreductase proteins. By in vitro crosslinking using native cysteine residues we show that ComEC forms an oligomer. The oligomerization surface includes a transmembrane segment, TMS-G, near the cytoplasmic C-terminus of ComEC.

Original languageEnglish (US)
Pages (from-to)881-896
Number of pages16
JournalMolecular microbiology
Volume55
Issue number3
DOIs
StatePublished - Feb 2005

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

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