scholarly journals Identification of an Acidic Amino Acid Permease Involved in d-Aspartate Uptake in the Yeast Cryptococcus humicola

2021 ◽  
Vol 9 (1) ◽  
pp. 192
Author(s):  
Daiki Imanishi ◽  
Yoshio Kera ◽  
Shouji Takahashi
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Yeast Genome ◽  
Acidic Amino Acid ◽  
Oxidative Deamination ◽  
Amino Acid Permease ◽  
Cryptococcus Humicola ◽  
Growth Defects ◽  
Alkaline Conditions ◽  
The Relationship

d-aspartate oxidase (DDO) catalyzes the oxidative deamination of acidic d-amino acids, and its production is induced by d-Asp in several eukaryotes. The yeast Cryptococcus humicola strain UJ1 produces large amounts of DDO (ChDDO) only in the presence of d-Asp. In this study, we analyzed the relationship between d-Asp uptake by an amino acid permease (Aap) and the inducible expression of ChDDO. We identified two acidic Aap homologs, named “ChAap4 and ChAap5,” in the yeast genome sequence. ChAAP4 deletion resulted in partial growth defects on d-Asp as well as l-Asp, l-Glu, and l-Phe at pH 7, whereas ChAAP5 deletion caused partial growth defects on l-Phe and l-Lys, suggesting that ChAap4 might participate in d-Asp uptake as an acidic Aap. Interestingly, the growth of the Chaap4 strain on d- or l-Asp was completely abolished at pH 10, suggesting that ChAap4 is the only Aap responsible for d- and l-Asp uptake under high alkaline conditions. In addition, ChAAP4 deletion significantly decreased the induction of DDO activity and ChDDO transcription in the presence of d-Asp. This study revealed that d-Asp uptake by ChAap4 might be involved in the induction of ChDDO expression by d-Asp.

scholarly journals 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

2002 ◽  
Vol 184 (15) ◽  
pp. 4071-4080 ◽  
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.

Self-healing hydrogels triggered by amino acids

2016 ◽  
Vol 3 (12) ◽  
pp. 1699-1704 ◽  
Author(s):  
Nicola Zanna ◽  
Andrea Merlettini ◽  
Claudia Tomasini
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Chemical Properties ◽  
Aromatic Amino Acids ◽  
Self Healing ◽  
Acidic Amino Acid ◽  
Basic Amino Acids

Nine amino acids with different chemical properties have been chosen to promote the formation of hydrogels based on the bolamphiphilic gelator A: three basic amino acids (arginine, histidine and lysine), one acidic amino acid (aspartic acid), two neutral aliphatic amino acids (alanine and serine) and three neutral aromatic amino acids (phenylalanine, tyrosine and tryptophan).

scholarly journals The Relationship between the Structure and Properties of Amino Acid Ionic Liquids

Molecules ◽  
2019 ◽  
Vol 24 (18) ◽  
pp. 3252 ◽  
Author(s):  
Paula Ossowicz ◽  
Joanna Klebeko ◽  
Barbara Roman ◽  
Ewa Janus ◽  
Zbigniew Rozwadowski
Keyword(s):  
Amino Acids ◽  
Ionic Liquids ◽  
Amino Acid ◽  
Surface Activity ◽  
Spectroscopic Properties ◽  
Specific Rotation ◽  
Structure And Properties ◽  
Rotation Surface ◽  
Cation Type ◽  
The Relationship

Ionic liquids based on different l-amino acids (glycine, l-valine, l-leucine, l-isoleucine, l-histidine, l-methionine, l-tyrosine, l-tryptophan, l-arginine, and l-threonine) and different cations (tetrabutylammonium (TBA), tributylmethylammonium (tBMA), didecyldimethylammonium (DDA), (2-hydroxyethyl)trimethylammonium (choline) (Chol), alkyl(C12-C14) dimethylbenzylammonium (benzalkonium) (BA), dodecyltrimethylammonium (DDTMA), hexadecyltrimethylammonium (HDTMA), octadecyltrimethylammonium (ODTMA) and 1-ethyl-3-methylimidazolium (EMIM)) have been synthesized and characterized by NMR and FTIR. Viscosity, specific rotation, surface activity, thermal stability (TG), and phase transformations (DSC) have been determined and compared with available data. Furthermore, benzalkonium, didecyldimethylammonium, dodecyltrimethylammonium, hexadecyltrimethylammonium, and octadecyltrimethylammonium amino acid ionic liquids have been shown to exhibit surface activity. The dissolution of cellulose in amino acid ionic liquids (AAILs) composed of various cations was also investigated. Cellulose was only dissolved in EMIM salts of amino acids. In particular, the influence of the cation type on selected physicochemical and spectroscopic properties were discussed. The article is a mini review on amino acid ionic liquids.

scholarly journals Regulation of the acidic amino acid permease of Aspergillus nidulans

1972 ◽  
Vol 127 (3) ◽  
pp. 71P-72P
Author(s):  
J H Robinson ◽  
C Anthony ◽  
W T Drabble
Keyword(s):  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Acidic Amino Acid ◽  
Amino Acid Permease

THE RELATIONSHIP BETWEEN SOIL BACTERIA WITH SIMPLE NUTRITIONAL REQUIREMENTS AND THOSE REQUIRING AMINO ACIDS

1957 ◽  
Vol 3 (1) ◽  
pp. 73-80 ◽  
Author(s):  
T. M. B. Payne ◽  
J. W. Rouatt ◽  
A. G. Lochhead
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Soil Bacteria ◽  
Single Case ◽  
The Other ◽  
Nutritional Requirements ◽  
Soil Organisms ◽  
Specific Amino Acid ◽  
The Relationship ◽  
Maximum Development

Twenty-two of 30 representative soil bacteria having simple nutritional requirements, in that they showed maximum development in a medium of inorganic salts and sugar, were found to be able to synthesize a variety of amino acids, though in no single case were more than four ninhydrin-positive substances found. The culture filtrates permitted the growth of amino-acid-requiring bacteria to the extent that they contained the specific amino acid or acids required by strains of the latter group. The findings point to an associative action between these nutritional groups of soil organisms and suggest that the preferential stimulation in the rhizosphere of bacteria requiring amino acids may be ascribed in part to the ability of the other group of bacteria, which are numerically increased in the rhizosphere, to synthesize amino acids.

N-Acetylglucosamine-inducible CaGAP1 encodes a general amino acid permease which co-ordinates external nitrogen source response and morphogenesis in Candida albicans

Microbiology ◽  
2003 ◽  
Vol 149 (9) ◽  
pp. 2597-2608 ◽  
Author(s):  
Subhrajit Biswas ◽  
Monideepa Roy ◽  
Asis Datta
Keyword(s):  
Amino Acids ◽  
Candida Albicans ◽  
Amino Acid ◽  
Genomic Library ◽  
Northern Analysis ◽  
Dependent Manner ◽  
Amino Acid Permease ◽  
Environmental Signals ◽  
General Amino Acid Permease ◽  
Hyphal Formation

Candida albicans is able to grow in a variety of reversible morphological forms (yeast, pseudohyphal and hyphal) in response to various environmental signals, noteworthy among them being N-acetylglucosamine (GlcNAc). The gene CaGAP1, homologous to GAP1, which encodes the general amino acid permease from Saccharomyces cerevisiae, was isolated on the basis of its induction by GlcNAc through differential screening of a C. albicans genomic library. The gene could functionally complement an S. cerevisiae gap1 mutant by rendering it susceptible to the toxic amino acid analogue mimosine in minimal proline media. As in S. cerevisiae, mutation of the CaGAP1 gene had an effect on citrulline uptake in C. albicans. Northern analysis showed that GlcNAc-induced expression of CaGAP1 was further enhanced in synthetic minimal media supplemented with single amino acids (glutamate, proline and glutamine) or urea (without amino acids) but repressed in minimal ammonium media. Induction of CaGAP1 expression by GlcNAc was nullified in C. albicans deleted for the transcription factor CPH1 and the hyphal regulator RAS1, indicating the involvement of Cph1p-dependent Ras1p signalling in CaGAP1 expression. A homozygous mutant of this gene showed defective hyphal formation in solid hyphal-inducing media and exhibited less hyphal clumps when induced by GlcNAc. Alteration of morphology and short filamentation under nitrogen-starvation conditions in the heterozygous mutant suggested that CaGAP1 affects morphogenesis in a dose-dependent manner.

scholarly journals The External Amino Acid Signaling Pathway Promotes Activation of Stp1 and Uga35/Dal81 Transcription Factors for Induction of the AGP1 Gene in Saccharomyces cerevisiae

Genetics ◽  
2004 ◽  
Vol 166 (4) ◽  
pp. 1727-1739 ◽  
Author(s):  
Fadi Abdel-Sater ◽  
Ismaïl Iraqui ◽  
Antonio Urrestarazu ◽  
Bruno André
Keyword(s):  
Amino Acids ◽  
Transcription Factor ◽  
Transcription Factors ◽  
Amino Acid ◽  
Signaling Pathway ◽  
Nitrogen Supply ◽  
Upstream Region ◽  
Gata Factor ◽  
Amino Acid Permease ◽  
Amino Acid Signaling

Abstract Yeast cells respond to the presence of amino acids in their environment by inducing transcription of several amino acid permease genes including AGP1, BAP2, and BAP3. The signaling pathway responsible for this induction involves Ssy1, a permease-like sensor of external amino acids, and culminates with proteolytic cleavage and translocation to the nucleus of the zinc-finger proteins Stp1 and Stp2, the lack of which abolishes induction of BAP2 and BAP3. Here we show that Stp1—but not Stp2—plays an important role in AGP1 induction, although significant induction of AGP1 by amino acids persists in stp1 and stp1 stp2 mutants. This residual induction depends on the Uga35/Dal81 transcription factor, indicating that the external amino acid signaling pathway activates not only Stp1 and Stp2, but also another Uga35/Dal81-dependent transcriptional circuit. Analysis of the AGP1 gene’s upstream region revealed that Stp1 and Uga35/Dal81 act synergistically through a 21-bp cis-acting sequence similar to the UASAA element previously found in the BAP2 and BAP3 upstream regions. Although cells growing under poor nitrogen-supply conditions display much higher induction of AGP1 expression than cells growing under good nitrogen-supply conditions, the UASAA itself is totally insensitive to nitrogen availability. Nitrogen-source control of AGP1 induction is mediated by the GATA factor Gln3, likely acting through adjacent 5′-GATA-3′ sequences, to amplify the positive effect of UASAA. Our data indicate that Stp1 may act in combination with distinct sets of transcription factors, according to the gene context, to promote induction of transcription in response to external amino acids. The data also suggest that Uga35/Dal81 is yet another transcription factor under the control of the external amino acid sensing pathway. Finally, the data show that the TOR pathway mediating global nitrogen control of transcription does not interfere with the external amino acid signaling pathway.

scholarly journals Evolutionary significance of amino acid permease transporters in 17 plants from Chlorophyta to Angiospermae

2020 ◽  
Author(s):  
Chao Zhang ◽  
Nana Kong ◽  
Minxuan Cao ◽  
Dongdong Wang ◽  
Yue Chen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Evolutionary Significance ◽  
Future Research ◽  
Amino Acid Permease ◽  
Group I ◽  
New Findings ◽  
Duplication Events ◽  
Living Organisms ◽  
Clade 1

Abstract Background: Nitrogen is an indispensable nutrient for plant growth. It is used and transported in the form of amino acids in living organisms. Transporting amino acids to various parts of plants requires relevant transport proteins, such as amino acid permeases (AAPs), which were our focus in this study.Results: We found that 5 AAP genes were present in Chlorophyte species and more AAP genes were predicted in Bryophyta and Lycophytes. Two main groups were defined and group I comprised 5 clades. Our phylogenetic analysis indicated that the origin of clades 2, 3, and 4 is Gymnospermae and that these clades are closely related. The members of clade 1 included Chlorophyta to Gymnospermae. Group II, as a new branch consisting of non-seed plants, is first proposed in our research. Our results also indicated that the AAP family was already present in Chlorophyta and then expanded accompanying the development of vasculature. Concurrently, the AAP family experienced multiple duplication events that promoted the generation of new functions and differentiation of sub-functions.Conclusions: Our findings suggest that the AAP gene originated in Chlorophyta, and some non-seed AAP genes clustered in one group. A second group, which contained plants of all evolutionary stages, indicated the evolution of AAPs. These new findings can be used to guide future research.

Amino acids in muscle and kidney of potassium-deficient rats

1960 ◽  
Vol 199 (1) ◽  
pp. 39-42 ◽  
Author(s):  
Ira K. Brandt ◽  
Victor A. Matalka ◽  
Jerome T. Combs
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Nitrogen ◽  
Potassium Deficiency ◽  
Experimental Diet ◽  
Basic Amino Acids ◽  
The Relationship ◽  
Predictable Variation

Muscle and kidney taken from rats with potassium-deficiency alkalosis contained a higher concentration of lysine, histidine and arginine than tissue taken from pair-fed control animals. The concentration of anserine, carnosine and alpha-amino nitrogen did not differ in the two groups. Although the concentration of virtually all of the above substances varied with the length of time that the animal had been receiving the experimental diet, the relationship between the data obtained from potassium-deficient animals and from the pair-fed controls remained constant. The results suggest that a mechanism other than replacement of lost potassium as cation may bring about the increase in the basic amino acids during potassium-deficiency alkalosis and that starvation is associated with a predictable variation in some of the amino acid constituents of the tissues.

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