Journal
MOLECULAR MICROBIOLOGY
Volume 55, Issue 3, Pages 881-896Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1365-2958.2004.04430.x
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Funding
- NIGMS NIH HHS [GM43756, R01 GM043756] Funding Source: Medline
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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.
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