The amino acid permease ( AAP ) genes CsAAP2A and SlAAP5A / B are required for oomycete susceptibility in cucumber and tomato

The activities of the proline-specific permease (PUT4) and the general amino acid permease (GAP1) of Saccharomyces cerevisiae vary 70- to 140-fold in response to the nitrogen source of the growth medium. The PUT4 and GAP1 permease activities are regulated by control of synthesis and control of activity. These permeases are irreversibly inactivated by addition of ammonia or glutamine, lowering the activity to that found during steady-state growth on these nitrogen sources. Mutants altered in the regulation of the PUT4 permease (Per-) have been isolated. The mutations in these strains are pleiotropic and affect many other permeases, but have no direct effect on various cytoplasmic enzymes involved in nitrogen assimilation. In strains having one class of mutations (per1), ammonia inactivation of the PUT4 and GAP1 permeases did not occur, whereas glutamate and glutamine inactivation did. Thus, there appear to be two independent inactivation systems, one responding to ammonia and one responding to glutamate (or a metabolite of glutamate). The mutations were found to be nuclear and recessive. The inactivation systems are constitutive and do not require transport of the effector molecules per se, apparently operating on the inside of the cytoplasmic membrane. The ammonia inactivation was found not to require a functional glutamate dehydrogenase (NADP). These mutants were used to show that ammonia exerts control of arginase synthesis largely by inducer exclusion. This may be the primary mode of nitrogen regulation for most nitrogen-regulated enzymes of S. cerevisiae.

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Relief from nitrogen starvation entails quick unexpected down-regulation of glycolytic/lipid metabolism genes in enologicalSaccharomyces cerevisiae

10.1101/428979 ◽

2018 ◽

Author(s):

Tesnière Catherine ◽

Bessière Chloé ◽

Pradal Martine ◽

Sanchez Isabelle ◽

Blondin Bruno ◽

...

Keyword(s):

Lipid Metabolism ◽

Amino Acid ◽

Wine Yeast ◽

Tca Cycle ◽

Nitrogen Addition ◽

White Wine ◽

Ammonium Nitrogen ◽

Ribosomal Protein Genes ◽

Amino Acid Permease ◽

Transcriptional Responses

AbstractNitrogen composition of the grape must has an impact on yeast growth and fermentation kinetics as well as on the organoleptic properties of the final product. In some technological processes, such as white wine/rosé winemaking, the yeast-assimilable nitrogen content is sometimes insufficient to cover yeast requirements, which can lead to slow or sluggish fermentations. Growth is nevertheless quickly restored upon relief from nutrient starvation, e.g. through the addition of ammonium nitrogen, allowing fermentation completion. The aim of this study was to determine how nitrogen repletion affected the transcriptional response of aSaccharomyces cerevisiaewine yeast strain, in particular within the first hour after nitrogen addition. We found almost 4800 genes induced or repressed, sometimes within minutes after nutrient changes. Some of these responses to nitrogen depended on the TOR pathway, which controls positively ribosomal protein genes, amino acid and purine biosynthesis or amino acid permease genes and negatively stress-response genes, and genes related to the retrograde response (RTG) specific to the tricarboxylic acid (TCA) cycle and nitrogen catabolite repression (NCR). Some unexpected transcriptional responses concerned all the glycolytic genes, carbohydrate metabolism and TCA cycle-related genes that were down-regulated, as well as genes from the lipid metabolism.

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Overexpression of Ubiquitin and Amino Acid Permease Genes in Association with Antimony Resistance in Leishmania tropica Field Isolates

The Korean Journal of Parasitology ◽

10.3347/kjp.2013.51.4.413 ◽

2013 ◽

Vol 51 (4) ◽

pp. 413-419 ◽

Cited By ~ 9

Author(s):

Elham Kazemi-Rad ◽

Mehdi Mohebali ◽

Mohammad Bagher Khadem-Erfan ◽

Homa Hajjaran ◽

Ramtin Hadighi ◽

...

Keyword(s):

Amino Acid ◽

Leishmania Tropica ◽

Amino Acid Permease ◽

Field Isolates ◽

Antimony Resistance

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Rhizobium leguminosarum Has a Second General Amino Acid Permease with Unusually Broad Substrate Specificity and High Similarity to Branched-Chain Amino Acid Transporters (Bra/LIV) of the ABC Family

Journal of Bacteriology ◽

10.1128/jb.184.15.4071-4080.2002 ◽

2002 ◽

Vol 184 (15) ◽

pp. 4071-4080 ◽

Cited By ~ 76

Author(s):

A. H. F. Hosie ◽

D. Allaway ◽

C. S. Galloway ◽

H. A. Dunsby ◽

P. S. Poole

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Rhizobium Leguminosarum ◽

Binding Protein ◽

Amino Acid Transporters ◽

Acid Uptake ◽

Amino Acid Permease ◽

Branched Chain Amino Acid ◽

General Amino Acid Permease ◽

Branched Chain

ABSTRACT Amino acid uptake by Rhizobium leguminosarum is dominated by two ABC transporters, the general amino acid permease (Aap) and the branched-chain amino acid permease (BraRl). Characterization of the solute specificity of BraRl shows it to be the second general amino acid permease of R. leguminosarum. Although BraRl has high sequence identity to members of the family of hydrophobic amino acid transporters (HAAT), it transports a broad range of solutes, including acidic and basic polar amino acids (l-glutamate, l-arginine, and l-histidine), in addition to neutral amino acids (l-alanine and l-leucine). While amino and carboxyl groups are required for transport, solutes do not have to be α-amino acids. Consistent with this, BraRl is the first ABC transporter to be shown to transport γ-aminobutyric acid (GABA). All previously identified bacterial GABA transporters are secondary carriers of the amino acid-polyamine-organocation (APC) superfamily. Also, transport by BraRl does not appear to be stereospecific as d amino acids cause significant inhibition of uptake of l-glutamate and l-leucine. Unlike all other solutes tested, l-alanine uptake is not dependent on solute binding protein BraCRl. Therefore, a second, unidentified solute binding protein may interact with the BraDEFGRl membrane complex during l-alanine uptake. Overall, the data indicate that BraRl is a general amino acid permease of the HAAT family. Furthermore, BraRl has the broadest solute specificity of any characterized bacterial amino acid transporter.

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Effects of ethanol and other alkanols on the general amino acid permease ofSaccharomyces cerevisiae

Biotechnology and Bioengineering ◽

10.1002/bit.260260422 ◽

1984 ◽

Vol 26 (4) ◽

pp. 403-405 ◽

Cited By ~ 43

Author(s):

Cecilia Leão ◽

N. van Uden

Keyword(s):

Amino Acid ◽

Amino Acid Permease ◽

General Amino Acid Permease

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Retraction Note to: Molecular Cloning of an Amino Acid Permease Gene and Structural Characterization of the Protein in Common Bean (Phaseolus vulgaris L.)

Molecular Biotechnology ◽

10.1007/s12033-020-00277-5 ◽

2020 ◽

Author(s):

Nibedita Chakraborty ◽

Alfred Besra ◽

Jolly Basak

Keyword(s):

Amino Acid ◽

Phaseolus Vulgaris ◽

Common Bean ◽

Molecular Cloning ◽

Structural Characterization ◽

Phaseolus Vulgaris L ◽

Amino Acid Permease

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Identification and Inactivation of Genetic Loci Involved with Lactobacillus acidophilus Acid Tolerance

Applied and Environmental Microbiology ◽

10.1128/aem.70.9.5315-5322.2004 ◽

2004 ◽

Vol 70 (9) ◽

pp. 5315-5322 ◽

Cited By ~ 97

Author(s):

M. Andrea Azcarate-Peril ◽

Eric Altermann ◽

Rebecca L. Hoover-Fitzula ◽

Raul J. Cano ◽

Todd R. Klaenhammer

Keyword(s):

Amino Acid ◽

Lactobacillus Acidophilus ◽

Acid Stress ◽

Acid Tolerance ◽

Low Ph ◽

Open Reading Frames ◽

Amino Acid Permease ◽

Physiological Limits ◽

Insertional Inactivation ◽

Genes Encoding

ABSTRACT Amino acid decarboxylation-antiporter reactions are one of the most important systems for maintaining intracellular pH between physiological limits under acid stress. We analyzed the Lactobacillus acidophilus NCFM complete genome sequence and selected four open reading frames with similarities to genes involved with decarboxylation reactions involved in acid tolerance in several microorganisms. Putative genes encoding an ornithine decarboxylase, an amino acid permease, a glutamate γ-aminobutyrate antiporter, and a transcriptional regulator were disrupted by insertional inactivation. The ability of L. acidophilus to survive low-pH conditions, such as those encountered in the stomach or fermented dairy foods, was investigated and compared to the abilities of early- and late-stationary-phase cells of the mutants by challenging them with a variety of acidic conditions. All of the integrants were more sensitive to low pH than the parental strain. Interestingly, each integrant also exhibited an adaptive acid response during logarithmic growth, indicating that multiple mechanisms are present and orchestrated in L. acidophilus in response to acid challenge.

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