title: The nucleobase-ascorbate transporter (NAT) family: genomics, evolution, structure-function relationships and physiological role.
abstract: This review summarizes knowledge concerning a ubiquitous plasma transmembrane protein family that mediates nucleobase or ascorbate secondary active transport (NAT). We show that prototype bacterial and mostly fungal members have become unique model systems to unravel structure-function relationships and regulation of expression, using classical and reverse genetics, as well as biochemical approaches. We discuss the importance of NAT-mediated ascorbate transport in mammals and how changes in substrate specificity, from different nucleobases to ascorbate, might have evolved at the molecular level. Finally, we also discuss how modelling NAT-purine interactions might constitute a step towards the use of NAT proteins as specific gateways for targeting pathogenic microbes.
authors.affiliation: Faculty of Biology, Department of Botany, University of Athens, Panepistimioupolis, Athens, Greece.
authors.forename: Christos
authors.initials: C
authors.lastname: Gournas
authors.forename: Ioannis
authors.initials: I
authors.lastname: Papageorgiou
authors.forename: George
authors.initials: G
authors.lastname: Diallinas
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001205:Ascorbic Acid / Q000378:metabolism*; D019143:Evolution, Molecular; D023281:Genomics; D006801:Humans; D008954:Models, Biological; D008969:Molecular Sequence Data; D033702:Nucleobase Transport Proteins / Q000502:physiology*; D016415:Sequence Alignment; D013329:Structure-Activity Relationship
chemical_list: D033702:Nucleobase Transport Proteins; D001205:Ascorbic Acid