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  • 1
    Electronic Resource
    Electronic Resource
    Voltage-sensitive ion channel ofEscherichia coli (1989)
    Springer
    The journal of membrane biology 112 (1989), S. 267-275 
    Details
    ISSN: 1432-1424
    Keywords: Escherichia coli ; outer membrane ; ion channel ; patch clamp ; porin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A voltage-sensitive, cation-selective ion channel ofEscherichia coli has been reconstituted into liposomes and studied with the patch-clamp method. The single channel conductance was 91 pS in symmetric solutions of 150mm KCl. Many channels were open most of the time, with frequent brief transitions to closed levels. Multiple conducting units could close and reopen simultaneously, and this apparent cooperativity in gating was increases with depolarizing voltages. Above a voltage threshold, the channels closed irreversibly, often in groups.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870957
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  • 2
    Electronic Resource
    Electronic Resource
    Activities of a Mechanosensitive Ion Channel in anE. Coli Mutant Lacking the Major Lipoprotein (1993)
    Springer
    The journal of membrane biology 131 (1993), S. 151-160 
    Details
    ISSN: 1432-1424
    Keywords: mechanosensitive channel ; outer membrane ; Escherichia coli/kw] ; lipoprotein ; membrane protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The activity of the mechanosensitive (MS) ion channels in membrane patches, excised fromE. coli spheroplasts, was analyzed using the patch-clamp technique. Outer membranes from a mutant lacking the major lipoprotein (Lpp) and its wildtype parent were examined. The MS-channel activities in the wild-type membrane rarely revealed substates at the time resolution used. These channels showed a stretch sensitivity indicated by the IISP (the suction for ane-fold increase in channel open probability) of 4.9 mm Hg suction. The MS-channel activities oflpp included a prominent substate and showed a weaker mechano-sensitivity with an 1/S p of 10.0 mm Hg. Whereas small amphipaths (chlorpromazine, trinitrophenol) or a larger amphipath (lysolecithin) all activated the MS channel in the wild-type membrane under minimal suction, only the larger lysolecithin could activate the MS channel in thelpp membranes. After lysolecithin addition, thelpp membrane became more effective in transmitting the stretch force to the MS channel, as indicated by a steepening of the Boltzmann curve. We discuss one interpretation of these results, in which the major lipoprotein serves as a natural amphipath inserted in the inner monolayer and the loss of this natural amphipath makes the bilayer less able to transmit the gating force.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02260105
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  • 3
    Electronic Resource
    Electronic Resource
    Interactions between gene products involved in divalent cation transport in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 303-311 
    Details
    ISSN: 1617-4623
    Keywords: Metal homeostasis ; Metal resistance ; Transport ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The COT1 and ZRC1 genes of Saccharomyces cerevisiae are structurally related dosage-dependent suppressors of metal toxicity. COT1 confers increased tolerance to high levels of cobalt; ZRC1 confers increased tolerance to high levels of zinc. The two genes are not linked and have been mapped; COT1 to chromosome XV and ZRC1 to chromosome XIII. Phenotypes related to metal homeostasis have been examined in strains with varied COT1 and ZRC1 gene doses. Overexpression of COT1 confers tolerance to moderately toxic levels of zinc and ZRC1 confers tolerance to moderately toxic levels of cobalt. Strains that carry null alleles at both loci are viable. The metal-hypersensitive phenotypes of mutations in either gene are largely unaffected by changes in dosage of the other. COT1 and ZRCI function independently in conferring tolerance to their respective metals, yet the uptake of cobalt ions by yeast cells is dependent on the gene dosage of ZRC1 as well as of COT1 Strains that overexpress ZRC1 have increased uptake of cobalt ions, while ZRCI null mutants exhibit decreased cobalt uptake. The defects in cobalt uptake due to mutations at COT1 and ZRC1 are additive, suggesting that the two genes are responsible for the majority of cobalt and zinc uptake in yeast cells. The function of either gene product seems to be more important in metal homeostasis than is the GRR1 gene product, which is also involved in metal metabolism. Mutations in the GRR1 gene have no effect on the cobalt-related phenotypes of strains that have altered gene dosage of either COT1 or ZRC1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00285458
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