AGP2 Encodes the Major Permease for High Affinity Polyamine Import in Saccharomyces cerevisiae

Aouida, Mustapha; Leduc, Anick; Poulin, Richard; Ramotar, Dindial

doi:10.1074/jbc.m503071200

Cited by 74 publications

(92 citation statements)

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“…It has recently been reported that GAP1 (15) and AGP2 (16) can catalyze the uptake of polyamines together with amino acids in yeast. However, polyamine uptake by these proteins was greatly decreased when amino acids were present in the medium.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, we reported that GAP1, located on the plasma membrane, can catalyze the uptake of putrescine and spermidine together with the uptake of amino acids (15). Although it has been reported that AGP2 can selectively catalyze the uptake of spermidine (16), there is also a report that AGP2 functions as an amino acid permease (17). In this study, we looked for proteins that can preferentially catalyze the uptake of polyamines in S. cerevisiae.…”

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confidence: 99%

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Polyamine Uptake by DUR3 and SAM3 in Saccharomyces cerevisiae

Uemura

Kashiwagi

Igarashi

2007

Journal of Biological Chemistry

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It has been reported that GAP1 and AGP2 catalyze the uptake of polyamines together with amino acids in Saccharomyces cerevisiae. We have looked for polyamine-preferential uptake proteins in S. cerevisiae. DUR3 catalyzed the uptake of polyamines together with urea, and SAM3 was found to catalyze the uptake of polyamines together with S-adenosylmethionine, glutamic acid, and lysine. Polyamine uptake was greatly decreased in both DUR3-and SAM3-deficient cells. The K m values for putrescine and spermidine of DUR3 were 479 and 21.2 M, respectively, and those of SAM3 were 433 and 20.7 M, respectively. Polyamine stimulation of cell growth of a polyamine requiring mutant, which is deficient in ornithine decarboxylase, was not influenced by the disruption of GAP1 and AGP2, but it was diminished by the disruption of DUR3 and SAM3. Furthermore, the polyamine stimulation of cell growth of a polyamine-requiring mutant was completely inhibited by the disruption of both DUR3 and SAM3. The results indicate that DUR3 and SAM3 are major polyamine uptake proteins in yeast. We previously reported that polyamine transport protein kinase 2 regulates polyamine transport. It was found that DUR3 (but not SAM3) was activated by phosphorylation of Thr 250 , Ser 251 , and Thr 684 by polyamine transport protein kinase 2.Polyamines (putrescine, spermidine, and spermine) in cells, which are essential for cell growth, are regulated by biosynthesis, degradation, and transport (1-4). With regard to polyamine transport, the properties of four polyamine transport systems were characterized in Escherichia coli (5-8). They include spermidine-preferential and putrescine-specific uptake systems as well as PotE (involved in the excretion of putrescine by a putrescine-ornithine antiporter activity) and CadB (involved in the excretion of cadaverine by a cadaverine-lysine antiporter activity). The former two transport systems function at neutral pH (2), whereas the latter two transport systems at acidic pH (9). In Saccharomyces cerevisiae, we identified four genes that encode polyamine excretion proteins TPO1-TPO4, mainly located on the plasma membrane (10 -12). We also found that UGA4 (located on vacuoles) can catalyze the uptake of ␥-aminobutyric acid and putrescine (13), and TPO5 (located on Golgi or post-Golgi secretory vesicles) can catalyze the excretion of polyamines (14). Furthermore, we reported that GAP1, located on the plasma membrane, can catalyze the uptake of putrescine and spermidine together with the uptake of amino acids (15). Although it has been reported that AGP2 can selectively catalyze the uptake of spermidine (16), there is also a report that AGP2 functions as an amino acid permease (17). In this study, we looked for proteins that can preferentially catalyze the uptake of polyamines in S. cerevisiae. We found that DUR3 can catalyze the uptake of polyamines together with urea, and SAM3 (which belongs to the family of amino acid polyamine-organocation transporters (18)) can catalyze the uptake of putrescine and spermidine together wit...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Polyamine Uptake by DUR3 and SAM3 in Saccharomyces cerevisiae

Uemura

Kashiwagi

Igarashi

2007

Journal of Biological Chemistry

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“…Significant quantities of polyamines may occur in the soil (54), plant phloem (2,13,21), and root nodules (22,23,40). Polyamine uptake has been studied in many microorganisms, including bacteria (27,34), yeasts (4,28), protozoans (26,35), and soil fungi (20,37). Polyamine uptake can be used to maintain cellular homeostasis, and uptake of polyamines by swimming P. sojae zoospores, heretofore believed to be dependent on internal stores until host contact (8,11,12), could increase zoospore survival and aid the development of the germinating cysts.…”

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confidence: 99%

Levels of Polyamines and Kinetic Characterization of Their Uptake in the Soybean Pathogen Phytophthora sojae

Chibucos

Morris

2006

Appl Environ Microbiol

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Polyamines are ubiquitous biologically active aliphatic cations that are at least transiently available in the soil from decaying organic matter. Our objectives in this study were to characterize polyamine uptake kinetics in Phytophthora sojae zoospores and to quantify endogenous polyamines in hyphae, zoospores, and soybean roots. Zoospores contained 10 times more free putrescine than spermidine, while hyphae contained only 4 times as much free putrescine as spermidine. Zoospores contained no conjugated putrescine, but conjugated spermidine was present. Hyphae contained both conjugated putrescine and spermidine at levels comparable to the hyphal free putrescine and spermidine levels. In soybean roots, cadaverine was the most abundant polyamine, but only putrescine efflux was detected. The selective efflux of putrescine suggests that the regulation of polyamine availability is part of the overall plant strategy to influence microbial growth in the rhizosphere. In zoospores, uptake experiments with [1,4-14 C]putrescine and [1,4-14 C]spermidine confirmed the existence of high-affinity polyamine transport for both polyamines. Putrescine uptake was reduced by high levels of exogenous spermidine, but spermidine uptake was not reduced by exogenous putrescine. These observations suggest that P. sojae zoospores express at least two high-affinity polyamine transporters, one that is spermidine specific and a second that is putrescine specific or putrescine preferential. Disruption of polyamine uptake or metabolism has major effects on a wide range of cellular activities in other organisms and has been proposed as a potential control strategy for Phytophthora. Inhibition of polyamine uptake may be a means of reducing the fitness of the zoospore along with subsequent developmental stages that precede infection.

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“…The molecular identity of any such polyamine transporter in the parasite remains elusive. Several known polyamine transporters, such as the bacterial Pot E (Kashiwagi et al, 2000), S. cerevisiae Agp2p (Aouida et al, 2005), UGA4 (Uemura et al, 2004) and L. major LmPot1 (Haider et al, 2005) are members of the amino acid/polyamine/organocation (APC) superfamily of transporters. While preliminary investigations…”

Section: Discussionmentioning

confidence: 99%

Polyamine uptake by the intraerythrocytic malaria parasite, Plasmodium falciparum

Niemand

Louw

Birkholtz

et al. 2012

International Journal for Parasitology

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Polyamines and the enzymes involved in their biosynthesis are present at high levels in rapidly proliferating cells, including cancer cells and protozoan parasites. Inhibition of polyamine biosynthesis in asexual blood-stage malaria parasites causes cytostatic arrest of parasite development under in vitro conditions, but does not cure infections in vivo. This may be due to replenishment of the parasite's intracellular polyamine pool via salvage of exogenous polyamines from the host. However the mechanism(s) of polyamine uptake by the intra-erythrocytic parasite are not well understood. In this study, the uptake of the polyamines putrescine and spermidine into Plasmodium falciparum parasites functionally isolated from their host erythrocyte were investigated using radioisotope flux techniques. Both putrescine and spermidine were taken up into isolated parasites via a temperature-dependent process that showed cross-competition between different polyamines. There was also some inhibition of polyamine uptake by basic amino acids. Inhibition of polyamine biosynthesis led to an increase in the total amount of putrescine and spermidine taken up from the extracellular medium. The uptake of putrescine and spermidine by isolated parasites was independent of extracellular Na + but increased with increasing external pH. Uptake also showed a marked dependence on the parasite's membrane potential, decreasing with membrane depolarization and increasing with membrane hyperpolarization. The data are consistent with polyamines being taken up into the parasite via an electrogenic uptake process, energized by the parasite's inwardly negative membrane potential.

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AGP2 Encodes the Major Permease for High Affinity Polyamine Import in Saccharomyces cerevisiae

Cited by 74 publications

References 62 publications

Polyamine Uptake by DUR3 and SAM3 in Saccharomyces cerevisiae

Polyamine Uptake by DUR3 and SAM3 in Saccharomyces cerevisiae

Levels of Polyamines and Kinetic Characterization of Their Uptake in the Soybean Pathogen Phytophthora sojae

Polyamine uptake by the intraerythrocytic malaria parasite, Plasmodium falciparum

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