Amino acid transport in plants

Fischer, W

doi:10.1016/s1360-1385(98)01231-x

Cited by 303 publications

(220 citation statements)

References 54 publications

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“…The use of sequence homology also enabled the identification of transporters from ESTs and genomic clones (Chen and Bush, 1997). Based on sequence similarities, the plant transporters can be classified into two major superfamilies (Fischer et al, 1998). ATF (amino acid transport family), the largest of these families, includes the AAP gene family (Fischer et al, 1995), transporters that prefer Pro (ProT) (Rentsch et al, 1996), Lys/ His transporters (LHT) (Chen and Bush, 1997), and AUX1-related proteins (Bennett et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

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Functional Characterization and Expression Analysis of the Amino Acid Permease RcAAP3 from Castor Bean1

Neelam¹,

Marvier

Hall

et al. 1999

Plant Physiology

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A polymerase chain reaction-based library screening procedure was used to isolate RcAAP3, an amino acid permease cDNA from castor bean (Ricinus communis). RcAAP3 is 1.7 kb in length, with an open reading frame that encodes a protein with a calculated molecular mass of 51 kD. Hydropathy analysis indicates that the RcAAP3 protein is highly hydrophobic in nature with nine to 11 putative transmembrane domains. RcAAP3-mediated uptake of citrulline in a yeast transport mutant showed saturable kinetics with a K m of 0.4 mM. Transport was higher at acidic pH and was inhibited by the protonophore carbonylcyanide-m-chlorophenylhydrazone, suggesting a proton-coupled transport mechanism. Citrulline uptake was strongly inhibited (72%) by the permeable sulfydryl reagent N-ethylmaleimide, but showed lower sensitivity (30% inhibition) to the nonpermeable reagent p-chloromercuribenzenesulfonic acid. Diethylpyrocarbonate, a histidine modifier, inhibited citrulline uptake by 80%. A range of amino acids inhibited citrulline uptake, suggesting that RcAAP3 may be a broad substrate permease that can transport neutral and basic amino acids with a lower affinity for acidic amino acids. Northern analysis indicated that RcAAP3 is widely expressed in source and sink tissues of castor bean, and that the pattern of expression is distinct from RcAAP1 and RcAAP2.

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Section: Discussionmentioning

confidence: 99%

“…This results largely from the isolation of the genes encoding amino acid permeases using complementation of yeast transport mutants (Fischer et al, 1998). The biochemical properties of the Arabidopsis amino acid permeases have been described in a number of cases (Fischer et al, 1995(Fischer et al, , 1998.…”

mentioning

confidence: 99%

Functional Characterization and Expression Analysis of the Amino Acid Permease RcAAP3 from Castor Bean1

Neelam¹,

Marvier

Hall

et al. 1999

Plant Physiology

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“…Phylogenetic analysis revealed that the three Arabidopsis ProTs form a subgroup within the ProT branch of the ATF1 (amino acid transporter family 1) gene family ( Fig. 1; Fischer et al, 1998;Wipf et al, 2002). Interestingly, ProT members from a single plant species always cluster together, indicating that duplication of the genes was a relatively recent event.…”

Section: Atprot3 Is a Novel Member Of The Aprot Gene Familymentioning

confidence: 99%

“…Phylogenetic relationship between the AtProTs and related proteins. The analysis was performed using the aligned protein sequences of the Arabidopsis ATF gene family that, in addition to the ProTs, contains several groups of amino acid permeases (AAPs, LHTs, ANT-like proteins) as well as potential auxin transporters (AUX1; Fischer et al, 1998;Chen et al, 2001;Wipf et al, 2002). Proteins from other plant species were included for the ProT-like and the At1g08230-like proteins.…”

Section: Atprot3 Is a Novel Member Of The Aprot Gene Familymentioning

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The AtProT Family. Compatible Solute Transporters with Similar Substrate Specificity But Differential Expression Patterns

Grallath

Weimar²,

Meyer³

et al. 2005

Plant Physiology

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149

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Proline transporters (ProTs) mediate transport of the compatible solutes Pro, glycine betaine, and the stress-induced compound g-aminobutyric acid. A new member of this gene family, AtProT3, was isolated from Arabidopsis (Arabidopsis thaliana), and its properties were compared to AtProT1 and AtProT2. Transient expression of fusions of AtProT and the green fluorescent protein in tobacco (Nicotiana tabacum) protoplasts revealed that all three AtProTs were localized at the plasma membrane. Expression in a yeast (Saccharomyces cerevisiae) mutant demonstrated that the affinity of all three AtProTs was highest for glycine betaine (K m 5 0.1-0.3 mM), lower for Pro (K m 5 0.4-1 mM), and lowest for g-aminobutyric acid (K m 5 4-5 mM). Relative quantification of the mRNA level using real-time PCR and analyses of transgenic plants expressing the b-glucuronidase (uidA) gene under control of individual AtProT promoters showed that the expression pattern of AtProTs are complementary. AtProT1 expression was found in the phloem or phloem parenchyma cells throughout the whole plant, indicative of a role in long-distance transport of compatible solutes. b-Glucuronidase activity under the control of the AtProT2 promoter was restricted to the epidermis and the cortex cells in roots, whereas in leaves, staining could be demonstrated only after wounding. In contrast, AtProT3 expression was restricted to the above-ground parts of the plant and could be localized to the epidermal cells in leaves. These results showed that, although intracellular localization, substrate specificity, and affinity are very similar, the transporters fulfill different roles in planta.

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Control of Primary Metabolism in Plants

Plaxton¹,

McManus²

2006

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Evaluation of the transcriptome and genome to inform the study of metabolic control in plants OLIVER THIMM, OLIVER E. BLÄSING, BJORN USADEL and YVES GIBON 2.3.3 Mitochondrial and chloroplast proteomes 2.3.4 Other subcellular proteomes 2.3.5 A stamp of authenticity for the subcellular protein postcode? 2.4 Quantitative analyses of the proteome 2.4.1 Examples of quantitative proteomics 2.4.2 The use of high-throughput measurements of enzyme activity as a proxy for quantitative proteomics 2.5 The use of proteomics to investigate post-translational modification of proteins 2.5.1 Systematic identification of phosphorylated proteins 2.5.2 Systematic identification of protein redox modifications 2.6 The use of proteomics to investigate protein-protein interactions 2.7 Future perspectives References

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Amino acid transport in plants

Cited by 303 publications

References 54 publications

Functional Characterization and Expression Analysis of the Amino Acid Permease RcAAP3 from Castor Bean1

Functional Characterization and Expression Analysis of the Amino Acid Permease RcAAP3 from Castor Bean1

The AtProT Family. Compatible Solute Transporters with Similar Substrate Specificity But Differential Expression Patterns

Control of Primary Metabolism in Plants

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