Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1993-4-5
pubmed:abstractText
At pH 5-6 ATP-depleted washed cell preparations of strain NC233-10b[pII4-9], in which the cytosine permease was overexpressed, absorbed cytosine, hypoxanthine or fluorocytosine stoichiometrically with, respectively, about 1, 1.4 and 5 proton equivalents. The cellular pH fell proportionately. The membrane depolarization caused by each compound was assayed in the presence of glucose with a voltage-sensitive dye and increased in the same order. Fluorocytosine significantly lowered the growth yield that a 'petite' strain of the yeast formed at limiting glucose concentrations. At pH 5.6 with extracellular [K+] below 1 mM, each of the three substrates was accumulated about 200-fold from a dilute solution at the expense of the proton gradient. This concentration ratio corresponds to a solute gradient (delta mu(s)) of 13 kJ mol-1. Raising [K+]o systematically lowered the substrate accumulation ratio and delta muH. The mean ratio delta mu(s)/delta muH was 0.82 for all three substrates. It was concluded that whereas the behaviour of cytosine approximated to that expected for a symport of unit proton stoichiometry, the absorption of protons with fluorocytosine and, to a lesser extent, hypoxanthine, was only partly conserved as useful work. A possible mechanism of this novel phenomenon is outlined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytosine, http://linkedlifedata.com/resource/pubmed/chemical/FCY2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Flucytosine, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Hypoxanthine, http://linkedlifedata.com/resource/pubmed/chemical/Hypoxanthines, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nucleobase Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Potassium, http://linkedlifedata.com/resource/pubmed/chemical/Proton Pumps, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0749-503X
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:geneSymbol
FCY2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1053-64
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:1293884-Adenosine Triphosphate, pubmed-meshheading:1293884-Biological Transport, Active, pubmed-meshheading:1293884-Carrier Proteins, pubmed-meshheading:1293884-Cytosine, pubmed-meshheading:1293884-Flucytosine, pubmed-meshheading:1293884-Glucose, pubmed-meshheading:1293884-Hypoxanthine, pubmed-meshheading:1293884-Hypoxanthines, pubmed-meshheading:1293884-Kinetics, pubmed-meshheading:1293884-Membrane Potentials, pubmed-meshheading:1293884-Membrane Transport Proteins, pubmed-meshheading:1293884-Models, Biological, pubmed-meshheading:1293884-Nucleobase Transport Proteins, pubmed-meshheading:1293884-Potassium, pubmed-meshheading:1293884-Proton Pumps, pubmed-meshheading:1293884-Recombinant Proteins, pubmed-meshheading:1293884-Saccharomyces cerevisiae, pubmed-meshheading:1293884-Saccharomyces cerevisiae Proteins
pubmed:year
1992
pubmed:articleTitle
Fluorocytosine causes uncoupled dissipation of the proton gradient and behaves as an imperfect substrate of the yeast cytosine permease.
pubmed:affiliation
Department of Biochemistry & Applied Molecular Biology, University of Manchester, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't