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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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Published in: | Journal of Amino Acids 2014 |
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container_title | Journal of Amino Acids |
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creator | Saenz, Daniel A Chianelli, Monica S Stella, Carlos A |
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. |
doi_str_mv | 10.1155/2014/283962 |
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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.</description><identifier>ISSN: 2090-0112</identifier><identifier>DOI: 10.1155/2014/283962</identifier><language>eng</language><publisher>John Wiley & Sons, Inc</publisher><subject>Biological transport ; Phenylalanine ; Physiological aspects ; Yeast fungi</subject><ispartof>Journal of Amino Acids, 2014</ispartof><rights>COPYRIGHT 2014 John Wiley & Sons, Inc.</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>776,780,4476,27902</link.rule.ids></links><search><creatorcontrib>Saenz, Daniel A</creatorcontrib><creatorcontrib>Chianelli, Monica S</creatorcontrib><creatorcontrib>Stella, Carlos A</creatorcontrib><title>L-phenylalanine transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1</title><title>Journal of Amino Acids</title><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.</description><subject>Biological transport</subject><subject>Phenylalanine</subject><subject>Physiological aspects</subject><subject>Yeast fungi</subject><issn>2090-0112</issn><fulltext>true</fulltext><rsrctype>report</rsrctype><creationdate>2014</creationdate><recordtype>report</recordtype><sourceid/><recordid>eNqVjcFqAjEURbOwUGld-QPvAxxNYkaNu7G0unAxYJcFecQ39cn4MiRDwb_vLPoDvXdx4MLhKjU1em5MWS6sNm5hN0u_siM1ttrrQhtjn9Uk55se4rwrvR-rr2PRXUkeLbYoLAR9QsldTD2wwAlDuGKK90egDIES_XBmpC3UmHoO3GHPUSA2sK9qM4NdVdsZoFyg2tfmVT012Gaa_PFFzT_eP98OxTe2dGZp4vAWhl7oziEKNTzslbMr55xfu-W_hV8QUE2k</recordid><startdate>20140101</startdate><enddate>20140101</enddate><creator>Saenz, Daniel A</creator><creator>Chianelli, Monica S</creator><creator>Stella, Carlos A</creator><general>John Wiley & Sons, Inc</general><scope/></search><sort><creationdate>20140101</creationdate><title>L-phenylalanine transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1</title><author>Saenz, Daniel A ; Chianelli, Monica S ; Stella, Carlos A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-gale_infotracacademiconefile_A4264449743</frbrgroupid><rsrctype>reports</rsrctype><prefilter>reports</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Biological transport</topic><topic>Phenylalanine</topic><topic>Physiological aspects</topic><topic>Yeast fungi</topic><toplevel>online_resources</toplevel><creatorcontrib>Saenz, Daniel A</creatorcontrib><creatorcontrib>Chianelli, Monica S</creatorcontrib><creatorcontrib>Stella, Carlos A</creatorcontrib></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saenz, Daniel A</au><au>Chianelli, Monica S</au><au>Stella, Carlos A</au><format>book</format><genre>unknown</genre><ristype>RPRT</ristype><atitle>L-phenylalanine transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1</atitle><jtitle>Journal of Amino Acids</jtitle><date>2014-01-01</date><risdate>2014</risdate><issn>2090-0112</issn><abstract>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.</abstract><pub>John Wiley & Sons, Inc</pub><doi>10.1155/2014/283962</doi></addata></record> |
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identifier | ISSN: 2090-0112 |
ispartof | Journal of Amino Acids, 2014 |
issn | 2090-0112 |
language | eng |
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source | Publicly Available Content Database; Wiley_OA刊; PubMed Central |
subjects | Biological transport Phenylalanine Physiological aspects Yeast fungi |
title | L-phenylalanine transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1 |
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