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Mechanisms and Functional Properties of Two Peptide Transporters, AtPTR2 and fPTR2
The Arabidopsis AtPTR2 and fungal fPTR2 genes, which encode H + /dipeptide cotransporters, belong to two different subgroups of the p eptide t ransporter ( PTR ) ( NRT1 ) family. In this study, the kinetics, substrate specificity, stoichiometry, and voltage dependence of these two transporters expre...
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| Published in: | The Journal of biological chemistry 2004-07, Vol.279 (29), p.30150-30157 |
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| container_title | The Journal of biological chemistry |
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| creator | Chiang, Chien-Sung Stacey, Gary Tsay, Yi-Fang |
| description | The Arabidopsis AtPTR2 and fungal fPTR2 genes, which encode H + /dipeptide cotransporters, belong to two different subgroups of the p eptide t ransporter ( PTR ) ( NRT1 ) family. In this study, the kinetics, substrate specificity, stoichiometry, and voltage dependence of these two transporters
expressed in Xenopus oocytes were investigated using the two-microelectrode voltage-clamp method. The results showed that: 1) although AtPTR2
belongs to the same PTR family subgroup as certain H + /nitrate cotransporters, neither AtPTR2 nor fPTR2 exhibited any nitrate transporting activity; 2) AtPTR2 and fPTR2 transported
a wide spectrum of dipeptides with apparent affinity constants in the range of 30 μ m to 3 m m , the affinity being dependent on the side chain structure of both the N- and C-terminal amino acids; 3) larger maximal currents
( I max ) were evoked by positively charged dipeptides in AtPTR2 - or fPTR2 -injected oocytes; 4) a major difference between AtPTR2 and fPTR2 was that, whereas fPTR2 exhibited low Ala-Asp â transporting activity, AtPTR2 transported Ala-Asp â as efficiently as some of the positively charged dipeptides; 5) kinetic analysis suggested that both fPTR2 and AtPTR2 transported
by a random binding, simultaneous transport mechanism. The results also showed that AtPTR2 and fPTR2 were quite distinct from
PepT1 and PepT2, two well characterized animal PTR transporters in terms of order of binding of substrate and proton(s), pH
sensitivity, and voltage dependence. |
| doi_str_mv | 10.1074/jbc.M405192200 |
| format | article |
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expressed in Xenopus oocytes were investigated using the two-microelectrode voltage-clamp method. The results showed that: 1) although AtPTR2
belongs to the same PTR family subgroup as certain H + /nitrate cotransporters, neither AtPTR2 nor fPTR2 exhibited any nitrate transporting activity; 2) AtPTR2 and fPTR2 transported
a wide spectrum of dipeptides with apparent affinity constants in the range of 30 μ m to 3 m m , the affinity being dependent on the side chain structure of both the N- and C-terminal amino acids; 3) larger maximal currents
( I max ) were evoked by positively charged dipeptides in AtPTR2 - or fPTR2 -injected oocytes; 4) a major difference between AtPTR2 and fPTR2 was that, whereas fPTR2 exhibited low Ala-Asp â transporting activity, AtPTR2 transported Ala-Asp â as efficiently as some of the positively charged dipeptides; 5) kinetic analysis suggested that both fPTR2 and AtPTR2 transported
by a random binding, simultaneous transport mechanism. The results also showed that AtPTR2 and fPTR2 were quite distinct from
PepT1 and PepT2, two well characterized animal PTR transporters in terms of order of binding of substrate and proton(s), pH
sensitivity, and voltage dependence.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M405192200</identifier><identifier>PMID: 15138259</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Arabidopsis ; Arabidopsis - metabolism ; Arabidopsis Proteins - chemistry ; Arabidopsis Proteins - physiology ; Biological Transport ; Cloning, Molecular ; DNA, Complementary - metabolism ; Electrophysiology ; Histidine - chemistry ; Humans ; Hydrogen-Ion Concentration ; Kinetics ; Membrane Potentials ; Membrane Transport Proteins - chemistry ; Membrane Transport Proteins - physiology ; Models, Biological ; Nitrates - chemistry ; Nitrates - metabolism ; Oocytes - metabolism ; Peptides - chemistry ; Phylogeny ; Protein Binding ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - physiology ; Substrate Specificity ; Xenopus</subject><ispartof>The Journal of biological chemistry, 2004-07, Vol.279 (29), p.30150-30157</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-7add2dcaf837bb56751f49123560563275bb318ccc026c58384fec8f6004a6ec3</citedby><cites>FETCH-LOGICAL-c457t-7add2dcaf837bb56751f49123560563275bb318ccc026c58384fec8f6004a6ec3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15138259$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chiang, Chien-Sung</creatorcontrib><creatorcontrib>Stacey, Gary</creatorcontrib><creatorcontrib>Tsay, Yi-Fang</creatorcontrib><title>Mechanisms and Functional Properties of Two Peptide Transporters, AtPTR2 and fPTR2</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The Arabidopsis AtPTR2 and fungal fPTR2 genes, which encode H + /dipeptide cotransporters, belong to two different subgroups of the p eptide t ransporter ( PTR ) ( NRT1 ) family. In this study, the kinetics, substrate specificity, stoichiometry, and voltage dependence of these two transporters
expressed in Xenopus oocytes were investigated using the two-microelectrode voltage-clamp method. The results showed that: 1) although AtPTR2
belongs to the same PTR family subgroup as certain H + /nitrate cotransporters, neither AtPTR2 nor fPTR2 exhibited any nitrate transporting activity; 2) AtPTR2 and fPTR2 transported
a wide spectrum of dipeptides with apparent affinity constants in the range of 30 μ m to 3 m m , the affinity being dependent on the side chain structure of both the N- and C-terminal amino acids; 3) larger maximal currents
( I max ) were evoked by positively charged dipeptides in AtPTR2 - or fPTR2 -injected oocytes; 4) a major difference between AtPTR2 and fPTR2 was that, whereas fPTR2 exhibited low Ala-Asp â transporting activity, AtPTR2 transported Ala-Asp â as efficiently as some of the positively charged dipeptides; 5) kinetic analysis suggested that both fPTR2 and AtPTR2 transported
by a random binding, simultaneous transport mechanism. The results also showed that AtPTR2 and fPTR2 were quite distinct from
PepT1 and PepT2, two well characterized animal PTR transporters in terms of order of binding of substrate and proton(s), pH
sensitivity, and voltage dependence.</description><subject>Animals</subject><subject>Arabidopsis</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - chemistry</subject><subject>Arabidopsis Proteins - physiology</subject><subject>Biological Transport</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - metabolism</subject><subject>Electrophysiology</subject><subject>Histidine - chemistry</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Membrane Potentials</subject><subject>Membrane Transport Proteins - chemistry</subject><subject>Membrane Transport Proteins - physiology</subject><subject>Models, Biological</subject><subject>Nitrates - chemistry</subject><subject>Nitrates - metabolism</subject><subject>Oocytes - metabolism</subject><subject>Peptides - chemistry</subject><subject>Phylogeny</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - physiology</subject><subject>Substrate Specificity</subject><subject>Xenopus</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqFkM9LwzAUx4Mobk6vHqUH8WRnfjRpehzDqbDhGBW8hTRNbUbb1KRl-N_bucGOvst7h8_38d4HgFsEpwjG0dM2U9NVBClKMIbwDIwR5CQkFH2egzGEGIUJpnwErrzfwqGiBF2CEaKIcEyTMdistCplY3ztA9nkwaJvVGdsI6tg7WyrXWe0D2wRpDsbrHXbmVwHqZONb63rtPOPwaxbpxv8ly720zW4KGTl9c2xT8DH4jmdv4bL95e3-WwZqojGXRjLPMe5kgUncZZRFlNUDNdhQhmkjOCYZhlBXCkFMVOUEx4VWvGCDU9IphWZgIfD3tbZ7177TtTGK11VstG294IxlkCMyb8g4oOYJEIDOD2AylnvnS5E60wt3Y9AUOx1i0G3OOkeAnfHzX1W6_yEH_0OwP0BKM1XuTNOi8xYVepa4DgROBEEIgrJLxO1hW8</recordid><startdate>20040716</startdate><enddate>20040716</enddate><creator>Chiang, Chien-Sung</creator><creator>Stacey, Gary</creator><creator>Tsay, Yi-Fang</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20040716</creationdate><title>Mechanisms and Functional Properties of Two Peptide Transporters, AtPTR2 and fPTR2</title><author>Chiang, Chien-Sung ; Stacey, Gary ; Tsay, Yi-Fang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c457t-7add2dcaf837bb56751f49123560563275bb318ccc026c58384fec8f6004a6ec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Arabidopsis</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis Proteins - chemistry</topic><topic>Arabidopsis Proteins - physiology</topic><topic>Biological Transport</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary - metabolism</topic><topic>Electrophysiology</topic><topic>Histidine - chemistry</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Membrane Potentials</topic><topic>Membrane Transport Proteins - chemistry</topic><topic>Membrane Transport Proteins - physiology</topic><topic>Models, Biological</topic><topic>Nitrates - chemistry</topic><topic>Nitrates - metabolism</topic><topic>Oocytes - metabolism</topic><topic>Peptides - chemistry</topic><topic>Phylogeny</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - physiology</topic><topic>Substrate Specificity</topic><topic>Xenopus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chiang, Chien-Sung</creatorcontrib><creatorcontrib>Stacey, Gary</creatorcontrib><creatorcontrib>Tsay, Yi-Fang</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chiang, Chien-Sung</au><au>Stacey, Gary</au><au>Tsay, Yi-Fang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mechanisms and Functional Properties of Two Peptide Transporters, AtPTR2 and fPTR2</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-07-16</date><risdate>2004</risdate><volume>279</volume><issue>29</issue><spage>30150</spage><epage>30157</epage><pages>30150-30157</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>The Arabidopsis AtPTR2 and fungal fPTR2 genes, which encode H + /dipeptide cotransporters, belong to two different subgroups of the p eptide t ransporter ( PTR ) ( NRT1 ) family. In this study, the kinetics, substrate specificity, stoichiometry, and voltage dependence of these two transporters
expressed in Xenopus oocytes were investigated using the two-microelectrode voltage-clamp method. The results showed that: 1) although AtPTR2
belongs to the same PTR family subgroup as certain H + /nitrate cotransporters, neither AtPTR2 nor fPTR2 exhibited any nitrate transporting activity; 2) AtPTR2 and fPTR2 transported
a wide spectrum of dipeptides with apparent affinity constants in the range of 30 μ m to 3 m m , the affinity being dependent on the side chain structure of both the N- and C-terminal amino acids; 3) larger maximal currents
( I max ) were evoked by positively charged dipeptides in AtPTR2 - or fPTR2 -injected oocytes; 4) a major difference between AtPTR2 and fPTR2 was that, whereas fPTR2 exhibited low Ala-Asp â transporting activity, AtPTR2 transported Ala-Asp â as efficiently as some of the positively charged dipeptides; 5) kinetic analysis suggested that both fPTR2 and AtPTR2 transported
by a random binding, simultaneous transport mechanism. The results also showed that AtPTR2 and fPTR2 were quite distinct from
PepT1 and PepT2, two well characterized animal PTR transporters in terms of order of binding of substrate and proton(s), pH
sensitivity, and voltage dependence.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15138259</pmid><doi>10.1074/jbc.M405192200</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS |
| subjects | Animals Arabidopsis Arabidopsis - metabolism Arabidopsis Proteins - chemistry Arabidopsis Proteins - physiology Biological Transport Cloning, Molecular DNA, Complementary - metabolism Electrophysiology Histidine - chemistry Humans Hydrogen-Ion Concentration Kinetics Membrane Potentials Membrane Transport Proteins - chemistry Membrane Transport Proteins - physiology Models, Biological Nitrates - chemistry Nitrates - metabolism Oocytes - metabolism Peptides - chemistry Phylogeny Protein Binding Protein Structure, Tertiary Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - physiology Substrate Specificity Xenopus |
| title | Mechanisms and Functional Properties of Two Peptide Transporters, AtPTR2 and fPTR2 |
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