| http://purl.uniprot.org/citations/10085225 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10085225 | http://www.w3.org/2000/01/rdf-schema#comment | "The transport of uracil into the yeast Saccharomyces cerevisiae is mediated by uracil permease, a specific co-transporter encoded by the FUR4 gene. Uracil permease is a multispan membrane protein that is delivered to the plasma membrane via the secretory pathway. Experimental results led to the proposal of a two-dimensional model of the protein's topology. According to this model, the membrane domain of Fur4p contains three charged amino acid residues (Glu-243, Lys-272 and Glu-539) that are conserved in the members of the FUR family of yeast transporters. We have previously shown that a mis-sense mutation leading to the replacement of Lys-272 by Glu severely impairs the function of uracil permease. In the present paper, the role of the three charged residues present in the membrane-spanning regions of Fur4p was further investigated by using site-directed mutagenesis. The variant permeases were correctly targeted to the plasma membrane and their stabilities were similar to that of the wild-type permease. The effect of the mutations was studied by measuring the uptake constants for uracil on whole cells and equilibrium binding parameters on plasma membrane-enriched fractions. We found no evidence for ionic interaction between either of the glutamic residues in transmembrane segments 3 and 9 and the lysine residue in transmembrane segment 4. Of the three charged residues, only Lys-272 was important for the transport activity of the transporter. Its replacement by Ala, Glu or even Arg strongly impaired both the binding and the translocation of uracil."xsd:string |
| http://purl.uniprot.org/citations/10085225 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3390037"xsd:string |
| http://purl.uniprot.org/citations/10085225 | http://purl.uniprot.org/core/author | "Pinson B."xsd:string |
| http://purl.uniprot.org/citations/10085225 | http://purl.uniprot.org/core/author | "Chevallier J."xsd:string |
| http://purl.uniprot.org/citations/10085225 | http://purl.uniprot.org/core/author | "Urban-Grimal D."xsd:string |
| http://purl.uniprot.org/citations/10085225 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10085225 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/10085225 | http://purl.uniprot.org/core/pages | "37-42"xsd:string |
| http://purl.uniprot.org/citations/10085225 | http://purl.uniprot.org/core/title | "Only one of the charged amino acids located in membrane-spanning regions is important for the function of the Saccharomyces cerevisiae uracil permease."xsd:string |
| http://purl.uniprot.org/citations/10085225 | http://purl.uniprot.org/core/volume | "339"xsd:string |
| http://purl.uniprot.org/citations/10085225 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10085225 |
| http://purl.uniprot.org/citations/10085225 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10085225 |
| http://purl.uniprot.org/uniprot/#_P05316-mappedCitation-10085225 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10085225 |
| http://purl.uniprot.org/uniprot/#_P38196-mappedCitation-10085225 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10085225 |
| http://purl.uniprot.org/uniprot/P05316 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10085225 |
| http://purl.uniprot.org/uniprot/P38196 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10085225 |