A single amino acid substitution alters conductance and gating of OmpC porin ofEscherichia coli View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-02

AUTHORS

Anne H. Delcour, Julius Adler, Ching Kung

ABSTRACT

We have reconstituted into liposomes outer-membrane fractions from Escherichia coli strains which express OmpC porins with altered pore properties. Single-channel experiments were performed with the patch-clamp technique on blisters generated from the reconstituted liposomes. Our goal was to identify positively the activity pattern of OmpC in our reconstituted system. The properties of the parent strain were compared to those of a strain whose OmpC porin has a single amino acid substitution in a postulated transmembrane segment. The parent and the mutant strain each exhibit a cation-selective channel of high open probability and gating to closed levels of various amplitudes. However, the mutant channel appeared to be 9 to 30% larger in unit conductance. It tended to close and reopen most often in groups of three units, as opposed to two units in the parent channel. The results are discussed in terms of the observed phenotype and of their implication as to the structure-function relationship of the porin channels. More... »

PAGES

267-275

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01868731

DOI

http://dx.doi.org/10.1007/bf01868731

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1007202574

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2056524


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