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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Krammer, Eva-maria Brohée, Sylvain André, Bruno Prévost, Martine Mihajlovic, Natalija Ghaddar, Kassem |
| Description | Author Affiliation: Ghaddar K ( From the Laboratoire de Physiologie Moléculaire de la Cellule CP300, Institut de Biologie et de Médecine Moléculaires (IBMM), Université Libre de Bruxelles (ULB), 11 Rue des Pr. Jeener et Brachet, 6041 Gosselies, Belgium.) |
| Abstract | Amino acid uptake in yeast cells is mediated by about 16 plasma membrane permeases, most of which belong to the amino acid-polyamine-organocation (APC) transporter family. These proteins display various substrate specificity ranges. For instance, the general amino acid permease Gap1 transports all amino acids, whereas Can1 and Lyp1 catalyze specific uptake of arginine and lysine, respectively. Although Can1 and Lyp1 have different narrow substrate specificities, they are close homologs. Here we investigated the molecular rules determining the substrate specificity of the H(+)-driven arginine-specific permease Can1. Using a Can1-Lyp1 sequence alignment as a guideline and a three-dimensional Can1 structural model based on the crystal structure of the bacterial APC family arginine/agmatine antiporter, we introduced amino acid substitutions liable to alter Can1 substrate specificity. We show that the single substitution T456S results in a Can1 variant transporting lysine in addition to arginine and that the combined substitutions T456S and S176N convert Can1 to a Lyp1-like permease. Replacement of a highly conserved glutamate in the Can1 binding site leads to variants (E184Q and E184A) incapable of any amino acid transport, pointing to a potential role for this glutamate in H(+) coupling. Measurements of the kinetic parameters of arginine and lysine uptake by the wild-type and mutant Can1 permeases, together with docking calculations for each amino acid in their binding site, suggest a model in which residues at positions 176 and 456 confer substrate selectivity at the ligand-binding stage and/or in the course of conformational changes required for transport. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 10 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-03-07 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Amino Acid Transport Systems, Basic Chemistry Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Enzymology Amino Acid Sequence Genetics Arginine Metabolism Binding Sites Biological Transport Imaging, Three-Dimensional Models, Chemical Molecular Sequence Data Mutagenesis, Site-Directed Protein Conformation Substrate Specificity Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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