Journal of Biological Chemistry · 1995 · 270 citations · 19 references
Life SciencesPlant BiologyPlant SciencesGene ExpressionPlant BiochemistryPlant Molecular BiologyMembrane TransportTransport Across Biological MembranesAmino Acid TransportAmino Acid Transporter SubstratesAmino AcidsConcentration Gradient Driven TransportMembrane-spanning DomainsSubstrate Binding SpecificitySubstrate Specificity ProfilingTransporters
Three amino acid transporter genes (AAP3-5) were isolated from Arabidopsis by complementation of a yeast mutant defective in histidine uptake. Transport is driven against a concentration gradient and sensitive to protonophores. Analysis of the substrate specificity demonstrates that the carriers have a broad substrate specificity covering the major transport forms of reduced nitrogen, i.e. glutamine and glutamate. The transporters have similar affinities for glutamate, glutamine, and alanine but differ with respect to valine, phenylalanine, histidine, arginine, and lysine. AAP3 and AAP5 efficiently transport arginine and lysine and are involved in basic amino acid transport. The predicted polypeptides of 53 kDa are highly hydrophobic with 12 putative membrane-spanning regions and show significant homologies to Arabidopsis amino acid transporters AAP1 and AAP2. Each of the genes has a different organ-specific expression in the plant. AAP3 is exclusively expressed in roots and AAP4 mainly in source leaves, stems, and flowers, whereas AAP5 is found in all tissues. The specific distribution in the plant and the different substrate specificities of AAP transporters may indicate that tissues differ both qualitatively and quantitatively regarding import or export of amino acids.
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A comprehensive set of sequence analysis programs for the VAX
John Devereux, Paul Haeberli, Oliver Smithies · Nucleic Acids Research · 1984 · 14.4K citations · Full text
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