delta-Aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease UGA4.
There is evidence that delta-aminolevulinic acid (ALA), a precursor of porphyrin biosynthesis, and gamma-aminobutyric acid (GABA) would be incorporated into yeast cells by a common permease. The purpose of this work was to confirm this hypothesis and to identify the shared permease. The transport of...
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1996
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01455680_v42_n4_p519_BermudezMoretti http://hdl.handle.net/20.500.12110/paper_01455680_v42_n4_p519_BermudezMoretti |
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paper:paper_01455680_v42_n4_p519_BermudezMoretti2023-06-08T15:12:19Z delta-Aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease UGA4. Bermudez Moretti, Mariana Correa García, Susana Raquel Ramos, Eugenia H. Batlle, Alcira María del Carmen 4 aminobutyric acid 4 aminobutyric acid carrier aminolevulinic acid carrier protein GABA permease organic anion transporter Saccharomyces cerevisiae protein UGA4 protein, S cerevisiae article enzyme specificity metabolism Saccharomyces cerevisiae Aminolevulinic Acid GABA Plasma Membrane Transport Proteins gamma-Aminobutyric Acid Membrane Transport Proteins Organic Anion Transporters Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Substrate Specificity There is evidence that delta-aminolevulinic acid (ALA), a precursor of porphyrin biosynthesis, and gamma-aminobutyric acid (GABA) would be incorporated into yeast cells by a common permease. The purpose of this work was to confirm this hypothesis and to identify the shared permease. The transport of GABA in Saccharomyces cerevisiae is mediated by three permeases: the general amino acid permease (GAP1), the specific proline permease (PUT4) and a fairly specific GABA permease (UGA4). To determine which of these permeases is also involved in ALA uptake, ALA and GABA incorporations were measured in strains lacking GAP1, UGA4 or GAP1 and UGA4 permeases. Results indicated that ALA is mainly incorporated by UGA4. This was also confirmed by regulatory studies, since ALA uptake was induced by GABA, and it is well known that UGA4 permease is induced by GABA. On the other hand, ALA did not induce the synthesis of this permease. Therefore, we demonstrate here that ALA, which cannot be used as a nitrogen source, is uptaken by S. cerevisiae cells mainly using a permease encoded by a gene subjected to a regulation typical of several nitrogen genes. Fil:Bermúdez Moretti, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Correa García, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 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. 1996 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01455680_v42_n4_p519_BermudezMoretti http://hdl.handle.net/20.500.12110/paper_01455680_v42_n4_p519_BermudezMoretti |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
4 aminobutyric acid 4 aminobutyric acid carrier aminolevulinic acid carrier protein GABA permease organic anion transporter Saccharomyces cerevisiae protein UGA4 protein, S cerevisiae article enzyme specificity metabolism Saccharomyces cerevisiae Aminolevulinic Acid GABA Plasma Membrane Transport Proteins gamma-Aminobutyric Acid Membrane Transport Proteins Organic Anion Transporters Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Substrate Specificity |
spellingShingle |
4 aminobutyric acid 4 aminobutyric acid carrier aminolevulinic acid carrier protein GABA permease organic anion transporter Saccharomyces cerevisiae protein UGA4 protein, S cerevisiae article enzyme specificity metabolism Saccharomyces cerevisiae Aminolevulinic Acid GABA Plasma Membrane Transport Proteins gamma-Aminobutyric Acid Membrane Transport Proteins Organic Anion Transporters Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Substrate Specificity Bermudez Moretti, Mariana Correa García, Susana Raquel Ramos, Eugenia H. Batlle, Alcira María del Carmen delta-Aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease UGA4. |
topic_facet |
4 aminobutyric acid 4 aminobutyric acid carrier aminolevulinic acid carrier protein GABA permease organic anion transporter Saccharomyces cerevisiae protein UGA4 protein, S cerevisiae article enzyme specificity metabolism Saccharomyces cerevisiae Aminolevulinic Acid GABA Plasma Membrane Transport Proteins gamma-Aminobutyric Acid Membrane Transport Proteins Organic Anion Transporters Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Substrate Specificity |
description |
There is evidence that delta-aminolevulinic acid (ALA), a precursor of porphyrin biosynthesis, and gamma-aminobutyric acid (GABA) would be incorporated into yeast cells by a common permease. The purpose of this work was to confirm this hypothesis and to identify the shared permease. The transport of GABA in Saccharomyces cerevisiae is mediated by three permeases: the general amino acid permease (GAP1), the specific proline permease (PUT4) and a fairly specific GABA permease (UGA4). To determine which of these permeases is also involved in ALA uptake, ALA and GABA incorporations were measured in strains lacking GAP1, UGA4 or GAP1 and UGA4 permeases. Results indicated that ALA is mainly incorporated by UGA4. This was also confirmed by regulatory studies, since ALA uptake was induced by GABA, and it is well known that UGA4 permease is induced by GABA. On the other hand, ALA did not induce the synthesis of this permease. Therefore, we demonstrate here that ALA, which cannot be used as a nitrogen source, is uptaken by S. cerevisiae cells mainly using a permease encoded by a gene subjected to a regulation typical of several nitrogen genes. |
author |
Bermudez Moretti, Mariana Correa García, Susana Raquel Ramos, Eugenia H. Batlle, Alcira María del Carmen |
author_facet |
Bermudez Moretti, Mariana Correa García, Susana Raquel Ramos, Eugenia H. Batlle, Alcira María del Carmen |
author_sort |
Bermudez Moretti, Mariana |
title |
delta-Aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease UGA4. |
title_short |
delta-Aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease UGA4. |
title_full |
delta-Aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease UGA4. |
title_fullStr |
delta-Aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease UGA4. |
title_full_unstemmed |
delta-Aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease UGA4. |
title_sort |
delta-aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease uga4. |
publishDate |
1996 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01455680_v42_n4_p519_BermudezMoretti http://hdl.handle.net/20.500.12110/paper_01455680_v42_n4_p519_BermudezMoretti |
work_keys_str_mv |
AT bermudezmorettimariana deltaaminolevulinicaciduptakeismediatedbythegammaaminobutyricacidspecificpermeaseuga4 AT correagarciasusanaraquel deltaaminolevulinicaciduptakeismediatedbythegammaaminobutyricacidspecificpermeaseuga4 AT ramoseugeniah deltaaminolevulinicaciduptakeismediatedbythegammaaminobutyricacidspecificpermeaseuga4 AT batllealciramariadelcarmen deltaaminolevulinicaciduptakeismediatedbythegammaaminobutyricacidspecificpermeaseuga4 |
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1768544589299318784 |