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L-Phenylalanine Transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1

We focused on the participation of GAP1, BAP2, and AGP1 in L-phenylalanine transport in yeast. In order to study the physiological functions of GAP1, BAP2, and AGP1 in L-phenylalanine transport, we examined the kinetics, substrate specificity, and regulation of these systems, employing isogenic hapl...

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Detalles Bibliográficos
Autores principales: Sáenz, Daniel A., Chianelli, Mónica S., Stella, Carlos A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3950631/
https://www.ncbi.nlm.nih.gov/pubmed/24701347
http://dx.doi.org/10.1155/2014/283962
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author Sáenz, Daniel A.
Chianelli, Mónica S.
Stella, Carlos A.
author_facet Sáenz, Daniel A.
Chianelli, Mónica S.
Stella, Carlos A.
author_sort Sáenz, Daniel A.
collection PubMed
description We focused on the participation of GAP1, BAP2, and AGP1 in L-phenylalanine transport in yeast. In order to study the physiological functions of GAP1, BAP2, and AGP1 in L-phenylalanine transport, we examined the kinetics, substrate specificity, and regulation of these systems, employing isogenic haploid strains with the respective genes disrupted individually and in combination. During the characterization of phenylalanine transport, we noted important regulatory phenomena associated with these systems. Our results show that Agp1p is the major transporter of the phenylalanine in a gap1 strain growing in synthetic media with leucine present as an inducer. In a wild type strain grown in the presence of leucine, when ammonium ion was the nitrogen source, Bap2p is the principal phenylalanine carrier.
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spelling pubmed-39506312014-04-03 L-Phenylalanine Transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1 Sáenz, Daniel A. Chianelli, Mónica S. Stella, Carlos A. J Amino Acids Research Article We focused on the participation of GAP1, BAP2, and AGP1 in L-phenylalanine transport in yeast. In order to study the physiological functions of GAP1, BAP2, and AGP1 in L-phenylalanine transport, we examined the kinetics, substrate specificity, and regulation of these systems, employing isogenic haploid strains with the respective genes disrupted individually and in combination. During the characterization of phenylalanine transport, we noted important regulatory phenomena associated with these systems. Our results show that Agp1p is the major transporter of the phenylalanine in a gap1 strain growing in synthetic media with leucine present as an inducer. In a wild type strain grown in the presence of leucine, when ammonium ion was the nitrogen source, Bap2p is the principal phenylalanine carrier. Hindawi Publishing Corporation 2014 2014-02-20 /pmc/articles/PMC3950631/ /pubmed/24701347 http://dx.doi.org/10.1155/2014/283962 Text en Copyright © 2014 Daniel A. Sáenz et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Sáenz, Daniel A.
Chianelli, Mónica S.
Stella, Carlos A.
L-Phenylalanine Transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1
title L-Phenylalanine Transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1
title_full L-Phenylalanine Transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1
title_fullStr L-Phenylalanine Transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1
title_full_unstemmed L-Phenylalanine Transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1
title_short L-Phenylalanine Transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1
title_sort l-phenylalanine transport in saccharomyces cerevisiae: participation of gap1, bap2, and agp1
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3950631/
https://www.ncbi.nlm.nih.gov/pubmed/24701347
http://dx.doi.org/10.1155/2014/283962
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