rdf:type |
|
lifeskim:mentions |
umls-concept:C0002812,
umls-concept:C0005495,
umls-concept:C0012854,
umls-concept:C0033684,
umls-concept:C0220781,
umls-concept:C0243144,
umls-concept:C0439799,
umls-concept:C0596901,
umls-concept:C1514873,
umls-concept:C1522492,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636
|
pubmed:issue |
3
|
pubmed:dateCreated |
2005-1-21
|
pubmed:abstractText |
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.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0950-382X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
55
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
881-96
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:15661011-Amino Acid Sequence,
pubmed-meshheading:15661011-Bacillus subtilis,
pubmed-meshheading:15661011-Bacterial Proteins,
pubmed-meshheading:15661011-Cell Membrane,
pubmed-meshheading:15661011-Computer Simulation,
pubmed-meshheading:15661011-Cysteine,
pubmed-meshheading:15661011-DNA-Binding Proteins,
pubmed-meshheading:15661011-Dimerization,
pubmed-meshheading:15661011-Disulfides,
pubmed-meshheading:15661011-Membrane Proteins,
pubmed-meshheading:15661011-Models, Molecular,
pubmed-meshheading:15661011-Molecular Sequence Data,
pubmed-meshheading:15661011-Protein Disulfide Reductase (Glutathione),
pubmed-meshheading:15661011-Transformation, Bacterial
|
pubmed:year |
2005
|
pubmed:articleTitle |
Biogenesis of a putative channel protein, ComEC, required for DNA uptake: membrane topology, oligomerization and formation of disulphide bonds.
|
pubmed:affiliation |
Public Health Research Institute at International Center for Public Health, 225 Warren Street, Newark, NJ 07103, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
|