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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
43
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pubmed:dateCreated |
1998-11-17
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pubmed:databankReference | |
pubmed:abstractText |
The cell wall of the Gram-positive bacterium Corynebacterium glutamicum contains a channel (porin) for the passage of hydrophilic solutes. The channel-forming protein was identified, by lipid bilayer experiments, in the cell envelope fractions isolated by sucrose-density centrifugations and in organic solvent of whole cells. It was purified to homogeneity by fast-protein liquid chromatography across a Mono-Q column. The pure protein had a rather low molecular mass of about 5 kDa as judged by SDS-PAGE, which suggested that the cell wall channel is formed by a protein oligomer. The monomer has according to partial sequencing no significant homology to known protein sequences. The purified protein formed large ion-permeable channels in lipid bilayer membranes from phosphatidylcholine/phosphatidylserine mixtures with a single-channel conductance of 5.5 nS in 1 M KCl. Experiments with different salts suggested that the cell wall channel of C. glutamicum was highly cation-selective caused by negative charges localized at the channel mouth. The analysis of the single-channel conductance data using the Renkin correction factor suggested that the diameter of the cell wall channel is about 2.2 nm. Channel-forming properties of the cell wall channel of C. glutamicum were compared with those of mycobacteria. These channels share common features because they form large and water-filled channels that contain point net charges.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase K,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Porins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15024-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9790664-Amino Acid Sequence,
pubmed-meshheading:9790664-Cell Membrane Permeability,
pubmed-meshheading:9790664-Cell Wall,
pubmed-meshheading:9790664-Corynebacterium,
pubmed-meshheading:9790664-Endopeptidase K,
pubmed-meshheading:9790664-Ion Channels,
pubmed-meshheading:9790664-Lipid Bilayers,
pubmed-meshheading:9790664-Membrane Potentials,
pubmed-meshheading:9790664-Molecular Sequence Data,
pubmed-meshheading:9790664-Molecular Weight,
pubmed-meshheading:9790664-Peptide Fragments,
pubmed-meshheading:9790664-Peptides,
pubmed-meshheading:9790664-Porins
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pubmed:year |
1998
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pubmed:articleTitle |
Biochemical and biophysical characterization of the cell wall porin of Corynebacterium glutamicum: the channel is formed by a low molecular mass polypeptide.
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pubmed:affiliation |
Lehrstuhl für Biotechnologie, Biozentrum der Universität Würzburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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