Carbon and nitrogen sources regulate δ-aminolevulinic acid and γ-aminobutyric acid transport in Saccharomyces cerevisiae
Evidence has been obtained showing that transport of S-aminolevulinic acid (ALA), a precursor of porphyrin biosynthesis in Saccharomyces cerevisiae, is mediated by the γ-aminobutyric acid (GABA)-specific permease, UGA4. In yeast GABA is also incorporated by the general amino acid permease (GAP1) and...
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1997
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13572725_v29_n8-9_p1097_Garci http://hdl.handle.net/20.500.12110/paper_13572725_v29_n8-9_p1097_Garci |
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paper:paper_13572725_v29_n8-9_p1097_Garci2023-06-08T16:11:15Z Carbon and nitrogen sources regulate δ-aminolevulinic acid and γ-aminobutyric acid transport in Saccharomyces cerevisiae Ramos, Eugenia H. Batlle, Alcira María del Carmen ALA GABA Saccharomyces cerevisiae Transport regulation UGA4 permease 4 aminobutyric acid aminolevulinic acid carbon nitrogen permease 4 aminobutyric acid uptake article controlled study nonhuman saccharomyces cerevisiae Aminolevulinic Acid Biological Transport Carbon Culture Media GABA Plasma Membrane Transport Proteins gamma-Aminobutyric Acid Kinetics Membrane Transport Proteins Nitrogen Organic Anion Transporters Proline Quaternary Ammonium Compounds Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Urea Saccharomyces cerevisiae Evidence has been obtained showing that transport of S-aminolevulinic acid (ALA), a precursor of porphyrin biosynthesis in Saccharomyces cerevisiae, is mediated by the γ-aminobutyric acid (GABA)-specific permease, UGA4. In yeast GABA is also incorporated by the general amino acid permease (GAP1) and the specific proline permease (PUT4). The aim of the present work was to carry out a comparative study on the regulation of ALA and GABA transport to confirm our proposal that both compounds share the UGA4 permease. ALA and GABA uptake were measured in cells grown on minimal media with different carbon and/or nitrogen sources. To study the effect of the carbon source on UGA4 permease, ALA and GABA incorporation mere measured in D27 strain, lacking GAP1 permease, and grown in proline as the sole nitrogen source, so the activity of PUT4 permease was negligible. The effect of the nitrogen source on UGA4 permease was studied measuring ALA and GABA uptake rates in cells from media with ammonium, proline and urea as nitrogen sources. It was found that the regulation by the carbon source was similar on ALA and GABA transport; they depend equally on the energetic conditions of the cells. Moreover, regulation by the nitrogen source on ALA and GABA uptake was also similar, and identical to that described already for UGA4 permease. These results are further evidence that both compounds, ALA and GABA, share the GABA-specific permease, UGA4. Fil:Ramos, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Batlle, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1997 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13572725_v29_n8-9_p1097_Garci http://hdl.handle.net/20.500.12110/paper_13572725_v29_n8-9_p1097_Garci |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
ALA GABA Saccharomyces cerevisiae Transport regulation UGA4 permease 4 aminobutyric acid aminolevulinic acid carbon nitrogen permease 4 aminobutyric acid uptake article controlled study nonhuman saccharomyces cerevisiae Aminolevulinic Acid Biological Transport Carbon Culture Media GABA Plasma Membrane Transport Proteins gamma-Aminobutyric Acid Kinetics Membrane Transport Proteins Nitrogen Organic Anion Transporters Proline Quaternary Ammonium Compounds Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Urea Saccharomyces cerevisiae |
spellingShingle |
ALA GABA Saccharomyces cerevisiae Transport regulation UGA4 permease 4 aminobutyric acid aminolevulinic acid carbon nitrogen permease 4 aminobutyric acid uptake article controlled study nonhuman saccharomyces cerevisiae Aminolevulinic Acid Biological Transport Carbon Culture Media GABA Plasma Membrane Transport Proteins gamma-Aminobutyric Acid Kinetics Membrane Transport Proteins Nitrogen Organic Anion Transporters Proline Quaternary Ammonium Compounds Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Urea Saccharomyces cerevisiae Ramos, Eugenia H. Batlle, Alcira María del Carmen Carbon and nitrogen sources regulate δ-aminolevulinic acid and γ-aminobutyric acid transport in Saccharomyces cerevisiae |
topic_facet |
ALA GABA Saccharomyces cerevisiae Transport regulation UGA4 permease 4 aminobutyric acid aminolevulinic acid carbon nitrogen permease 4 aminobutyric acid uptake article controlled study nonhuman saccharomyces cerevisiae Aminolevulinic Acid Biological Transport Carbon Culture Media GABA Plasma Membrane Transport Proteins gamma-Aminobutyric Acid Kinetics Membrane Transport Proteins Nitrogen Organic Anion Transporters Proline Quaternary Ammonium Compounds Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Urea Saccharomyces cerevisiae |
description |
Evidence has been obtained showing that transport of S-aminolevulinic acid (ALA), a precursor of porphyrin biosynthesis in Saccharomyces cerevisiae, is mediated by the γ-aminobutyric acid (GABA)-specific permease, UGA4. In yeast GABA is also incorporated by the general amino acid permease (GAP1) and the specific proline permease (PUT4). The aim of the present work was to carry out a comparative study on the regulation of ALA and GABA transport to confirm our proposal that both compounds share the UGA4 permease. ALA and GABA uptake were measured in cells grown on minimal media with different carbon and/or nitrogen sources. To study the effect of the carbon source on UGA4 permease, ALA and GABA incorporation mere measured in D27 strain, lacking GAP1 permease, and grown in proline as the sole nitrogen source, so the activity of PUT4 permease was negligible. The effect of the nitrogen source on UGA4 permease was studied measuring ALA and GABA uptake rates in cells from media with ammonium, proline and urea as nitrogen sources. It was found that the regulation by the carbon source was similar on ALA and GABA transport; they depend equally on the energetic conditions of the cells. Moreover, regulation by the nitrogen source on ALA and GABA uptake was also similar, and identical to that described already for UGA4 permease. These results are further evidence that both compounds, ALA and GABA, share the GABA-specific permease, UGA4. |
author |
Ramos, Eugenia H. Batlle, Alcira María del Carmen |
author_facet |
Ramos, Eugenia H. Batlle, Alcira María del Carmen |
author_sort |
Ramos, Eugenia H. |
title |
Carbon and nitrogen sources regulate δ-aminolevulinic acid and γ-aminobutyric acid transport in Saccharomyces cerevisiae |
title_short |
Carbon and nitrogen sources regulate δ-aminolevulinic acid and γ-aminobutyric acid transport in Saccharomyces cerevisiae |
title_full |
Carbon and nitrogen sources regulate δ-aminolevulinic acid and γ-aminobutyric acid transport in Saccharomyces cerevisiae |
title_fullStr |
Carbon and nitrogen sources regulate δ-aminolevulinic acid and γ-aminobutyric acid transport in Saccharomyces cerevisiae |
title_full_unstemmed |
Carbon and nitrogen sources regulate δ-aminolevulinic acid and γ-aminobutyric acid transport in Saccharomyces cerevisiae |
title_sort |
carbon and nitrogen sources regulate δ-aminolevulinic acid and γ-aminobutyric acid transport in saccharomyces cerevisiae |
publishDate |
1997 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13572725_v29_n8-9_p1097_Garci http://hdl.handle.net/20.500.12110/paper_13572725_v29_n8-9_p1097_Garci |
work_keys_str_mv |
AT ramoseugeniah carbonandnitrogensourcesregulatedaminolevulinicacidandgaminobutyricacidtransportinsaccharomycescerevisiae AT batllealciramariadelcarmen carbonandnitrogensourcesregulatedaminolevulinicacidandgaminobutyricacidtransportinsaccharomycescerevisiae |
_version_ |
1768541718653698048 |