| http://purl.uniprot.org/citations/20663086 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20663086 | http://www.w3.org/2000/01/rdf-schema#comment | "Al³+ -resistant cultivars of wheat (Triticum aestivum L.) release malate through the Al³+ -activated anion transport protein Triticum aestivum aluminum-activated malate transporter 1 (TaALMT1). Expression of TaALMT1 in Xenopus oocytes and tobacco suspension cells enhances the basal transport activity (inward and outward currents present in the absence of external Al³+, and generates the same Al³+ -activated currents (reflecting the Al³+-dependent transport function) as observed in wheat cells. We investigated the amino acid residues involved in this Al³+-dependent transport activity by generating a series of mutations to the TaALMT1 protein. We targeted the acidic residues on the hydrophilic C-terminal domain of TaALMT1 and changed them to uncharged residues by site-directed mutagenesis. These mutant proteins were expressed in Xenopus oocytes and their transport activity was measured before and after Al³+ addition. Three mutations (E274Q, D275N and E284Q) abolished the Al³+-activated transport activity without affecting the basal transport activity. Truncation of the hydrophilic C-terminal domain abolished both basal and Al³+-activated transport activities. Al³+-dependent transport activity was recovered by fusing the N-terminal region of TaALMT1 with the C-terminal region of AtALMT1, a homolog from Arabidopsis. These findings demonstrate that the extracellular C-terminal domain is required for both basal and Al³+-dependent TaALMT1 activity. Furthermore, we identified three acidic amino acids within this domain that are specifically required for the activation of transport function by external Al³+."xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1365-313x.2010.04309.x"xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/author | "Sasaki T."xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/author | "Tsuchiya Y."xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/author | "Yamamoto Y."xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/author | "Furuichi T."xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/author | "Delhaize E."xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/author | "Ryan P.R."xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/name | "Plant J"xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/pages | "47-55"xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/title | "An extracellular hydrophilic carboxy-terminal domain regulates the activity of TaALMT1, the aluminum-activated malate transport protein of wheat."xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://purl.uniprot.org/core/volume | "64"xsd:string |
| http://purl.uniprot.org/citations/20663086 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20663086 |
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