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Mol Microbiol. 2005 Feb;55(3):881-96.

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

Author information

1
Public Health Research Institute at International Center for Public Health, 225 Warren Street, Newark, NJ 07103, USA.

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 cross-linking 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.

PMID:
15661011
PMCID:
PMC3835657
DOI:
10.1111/j.1365-2958.2004.04430.x
[Indexed for MEDLINE]
Free PMC Article

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