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Identification and characterization of a third thioredoxin h in poplar
Three full-length sequences encoding thioredoxin h have been isolated in a leaf/root of Populus trichocarpa cv. Trichobel expressed sequence tag (EST) library. One of these, popCXXS1 exhibits the nontypical active site CXXS homologous to atCXXS1. The second one, named popTrxh4, is related to atTrxh9...
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| Published in: | Plant physiology and biochemistry 2003-06, Vol.41 (6), p.629-635 |
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| Main Authors: | , , , , , , , |
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| container_end_page | 635 |
| container_issue | 6 |
| container_start_page | 629 |
| container_title | Plant physiology and biochemistry |
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| creator | Gelhaye, Eric Rouhier, Nicolas Vlamis-Gardikas, Alexios Girardet, Jean-Michel Sautière, Pierre-Eric Sayzet, Michel Martin, Francis Jacquot, Jean-Pierre |
| description | Three full-length sequences encoding thioredoxin
h have been isolated in a leaf/root of
Populus trichocarpa cv.
Trichobel expressed sequence tag (EST) library. One of these, popCXXS1 exhibits the nontypical active site CXXS homologous to atCXXS1. The second one, named popTrxh4, is related to atTrxh9 which forms with several other plant thioredoxin
h a distinct subgroup of thioredoxins
h. The third one, named popTrxh3, displays 66% identity and also a high degree of homology (81%) vs. the previously described popTrxh1. Nevertheless, the active sites of both proteins differ, since the active site of popTrxh1 (WCPPC) is a variant of the canonical WCGPC found in popTrxh3. The cDNA sequence of popTrxh3 has been introduced in an expression plasmid (pET3d) in order to express the corresponding recombinant polypeptide. The protein has been expressed to a high level, purified from
Escherichia coli cells with a high yield and its catalytic properties compared to popTrxh1. Furthermore, two mutants, popTrxh1P40G and popTrxh3G41P, have been engineered in order to explore the importance of the active site residues in the thioredoxin
h catalytic properties. The results are discussed in relation with known biochemical properties of thioredoxins
h. |
| doi_str_mv | 10.1016/S0981-9428(03)00063-9 |
| format | article |
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h have been isolated in a leaf/root of
Populus trichocarpa cv.
Trichobel expressed sequence tag (EST) library. One of these, popCXXS1 exhibits the nontypical active site CXXS homologous to atCXXS1. The second one, named popTrxh4, is related to atTrxh9 which forms with several other plant thioredoxin
h a distinct subgroup of thioredoxins
h. The third one, named popTrxh3, displays 66% identity and also a high degree of homology (81%) vs. the previously described popTrxh1. Nevertheless, the active sites of both proteins differ, since the active site of popTrxh1 (WCPPC) is a variant of the canonical WCGPC found in popTrxh3. The cDNA sequence of popTrxh3 has been introduced in an expression plasmid (pET3d) in order to express the corresponding recombinant polypeptide. The protein has been expressed to a high level, purified from
Escherichia coli cells with a high yield and its catalytic properties compared to popTrxh1. Furthermore, two mutants, popTrxh1P40G and popTrxh3G41P, have been engineered in order to explore the importance of the active site residues in the thioredoxin
h catalytic properties. The results are discussed in relation with known biochemical properties of thioredoxins
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h have been isolated in a leaf/root of
Populus trichocarpa cv.
Trichobel expressed sequence tag (EST) library. One of these, popCXXS1 exhibits the nontypical active site CXXS homologous to atCXXS1. The second one, named popTrxh4, is related to atTrxh9 which forms with several other plant thioredoxin
h a distinct subgroup of thioredoxins
h. The third one, named popTrxh3, displays 66% identity and also a high degree of homology (81%) vs. the previously described popTrxh1. Nevertheless, the active sites of both proteins differ, since the active site of popTrxh1 (WCPPC) is a variant of the canonical WCGPC found in popTrxh3. The cDNA sequence of popTrxh3 has been introduced in an expression plasmid (pET3d) in order to express the corresponding recombinant polypeptide. The protein has been expressed to a high level, purified from
Escherichia coli cells with a high yield and its catalytic properties compared to popTrxh1. Furthermore, two mutants, popTrxh1P40G and popTrxh3G41P, have been engineered in order to explore the importance of the active site residues in the thioredoxin
h catalytic properties. The results are discussed in relation with known biochemical properties of thioredoxins
h.</description><subject>Biochemistry, Molecular Biology</subject><subject>CHEMICOPHYSICAL PROPERTIES</subject><subject>COMPOSÉ ORGANOSOUFRÉ</subject><subject>COMPUESTO ORGÁNICO DEL AZUFRE</subject><subject>Life Sciences</subject><subject>Medicin och hälsovetenskap</subject><subject>MUTANT</subject><subject>MUTANTES</subject><subject>MUTANTS</subject><subject>NUCLEOTIDE SEQUENCE</subject><subject>ORGANOSULPHUR COMPOUNDS</subject><subject>OXIDOREDUCTIONS</subject><subject>OXIRREDUCIÓN</subject><subject>OXYDORÉDUCTION</subject><subject>POPULUS</subject><subject>POTENCIAL REDOX</subject><subject>POTENTIEL REDOX</subject><subject>PROPIEDADES FISICOQUÍMICAS</subject><subject>PROPRIÉTÉ PHYSICOCHIMIQUE</subject><subject>PROTEINS</subject><subject>PROTEÍNAS</subject><subject>PROTÉINE</subject><subject>RECOMBINACIÓN</subject><subject>RECOMBINAISON</subject><subject>Recombinant</subject><subject>RECOMBINATION</subject><subject>REDOX POTENTIAL</subject><subject>Redox regulation</subject><subject>SECUENCIA NUCLEOTÍDICA</subject><subject>SÉQUENCE NUCLÉOTIDIQUE</subject><subject>Thioredoxin h</subject><issn>0981-9428</issn><issn>1873-2690</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNqFkU1r3DAQhkVoodu0PyHgY3JwK1nWSDqVELpNYCGQj7OQpVFW7cYyspO0_fWV4zQlh5LLSMw8jwTzEnLA6CdGGXy-pFqxWreNOqT8iFIKvNZ7ZMWU5HUDmr4hq2fkHXk_jt8L1LSSr8j6zGM_xRCdnWLqK9v7ym1ttm7CHH8vzRQqW03bmP1cU0affsa-2lalDGnY2fyBvA12N-LHp3OfXK-_Xp2c1pvzb2cnx5vaCQZT3XrsVMMbSiVoDkpKD9AADQJbaTHw1nXBK-FoCK23AhACOtlp66FTgvJ9Ui_vjg843HVmyPHW5l8m2WieWj_KDQ0wLkAUXv2XH3Ly_6S_ItNcKwBV1KNF3drdC-_0eGPmHm1ACtWwe1ZYsbAup3HMGJ4FRs2ckXnMyMwBGMrNY0ZGF-9g8YJNxt7kOJr1RdlOW-Jhcp5_WeZYdnofMZvRRewd-pjRTcan-MoPfwA2fKLx</recordid><startdate>20030601</startdate><enddate>20030601</enddate><creator>Gelhaye, Eric</creator><creator>Rouhier, Nicolas</creator><creator>Vlamis-Gardikas, Alexios</creator><creator>Girardet, Jean-Michel</creator><creator>Sautière, Pierre-Eric</creator><creator>Sayzet, Michel</creator><creator>Martin, Francis</creator><creator>Jacquot, Jean-Pierre</creator><general>Elsevier Masson SAS</general><general>Elsevier</general><scope>FBQ</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>1XC</scope><scope>ADTPV</scope><scope>AOWAS</scope><orcidid>https://orcid.org/0000-0002-0699-9113</orcidid><orcidid>https://orcid.org/0000-0003-4975-8587</orcidid><orcidid>https://orcid.org/0000-0002-2036-7884</orcidid></search><sort><creationdate>20030601</creationdate><title>Identification and characterization of a third thioredoxin h in poplar</title><author>Gelhaye, Eric ; Rouhier, Nicolas ; Vlamis-Gardikas, Alexios ; Girardet, Jean-Michel ; Sautière, Pierre-Eric ; Sayzet, Michel ; Martin, Francis ; Jacquot, Jean-Pierre</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c516t-4deb82320076936877d66260f5e47aef34cbfd85c0ff4da56e6fec7b9ad6b8503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Biochemistry, Molecular Biology</topic><topic>CHEMICOPHYSICAL PROPERTIES</topic><topic>COMPOSÉ ORGANOSOUFRÉ</topic><topic>COMPUESTO ORGÁNICO DEL AZUFRE</topic><topic>Life Sciences</topic><topic>Medicin och hälsovetenskap</topic><topic>MUTANT</topic><topic>MUTANTES</topic><topic>MUTANTS</topic><topic>NUCLEOTIDE SEQUENCE</topic><topic>ORGANOSULPHUR COMPOUNDS</topic><topic>OXIDOREDUCTIONS</topic><topic>OXIRREDUCIÓN</topic><topic>OXYDORÉDUCTION</topic><topic>POPULUS</topic><topic>POTENCIAL REDOX</topic><topic>POTENTIEL REDOX</topic><topic>PROPIEDADES FISICOQUÍMICAS</topic><topic>PROPRIÉTÉ PHYSICOCHIMIQUE</topic><topic>PROTEINS</topic><topic>PROTEÍNAS</topic><topic>PROTÉINE</topic><topic>RECOMBINACIÓN</topic><topic>RECOMBINAISON</topic><topic>Recombinant</topic><topic>RECOMBINATION</topic><topic>REDOX POTENTIAL</topic><topic>Redox regulation</topic><topic>SECUENCIA NUCLEOTÍDICA</topic><topic>SÉQUENCE NUCLÉOTIDIQUE</topic><topic>Thioredoxin h</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gelhaye, Eric</creatorcontrib><creatorcontrib>Rouhier, Nicolas</creatorcontrib><creatorcontrib>Vlamis-Gardikas, Alexios</creatorcontrib><creatorcontrib>Girardet, Jean-Michel</creatorcontrib><creatorcontrib>Sautière, Pierre-Eric</creatorcontrib><creatorcontrib>Sayzet, Michel</creatorcontrib><creatorcontrib>Martin, Francis</creatorcontrib><creatorcontrib>Jacquot, Jean-Pierre</creatorcontrib><collection>AGRIS</collection><collection>CrossRef</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>SwePub</collection><collection>SwePub Articles</collection><jtitle>Plant physiology and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gelhaye, Eric</au><au>Rouhier, Nicolas</au><au>Vlamis-Gardikas, Alexios</au><au>Girardet, Jean-Michel</au><au>Sautière, Pierre-Eric</au><au>Sayzet, Michel</au><au>Martin, Francis</au><au>Jacquot, Jean-Pierre</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of a third thioredoxin h in poplar</atitle><jtitle>Plant physiology and biochemistry</jtitle><date>2003-06-01</date><risdate>2003</risdate><volume>41</volume><issue>6</issue><spage>629</spage><epage>635</epage><pages>629-635</pages><issn>0981-9428</issn><eissn>1873-2690</eissn><abstract>Three full-length sequences encoding thioredoxin
h have been isolated in a leaf/root of
Populus trichocarpa cv.
Trichobel expressed sequence tag (EST) library. One of these, popCXXS1 exhibits the nontypical active site CXXS homologous to atCXXS1. The second one, named popTrxh4, is related to atTrxh9 which forms with several other plant thioredoxin
h a distinct subgroup of thioredoxins
h. The third one, named popTrxh3, displays 66% identity and also a high degree of homology (81%) vs. the previously described popTrxh1. Nevertheless, the active sites of both proteins differ, since the active site of popTrxh1 (WCPPC) is a variant of the canonical WCGPC found in popTrxh3. The cDNA sequence of popTrxh3 has been introduced in an expression plasmid (pET3d) in order to express the corresponding recombinant polypeptide. The protein has been expressed to a high level, purified from
Escherichia coli cells with a high yield and its catalytic properties compared to popTrxh1. Furthermore, two mutants, popTrxh1P40G and popTrxh3G41P, have been engineered in order to explore the importance of the active site residues in the thioredoxin
h catalytic properties. The results are discussed in relation with known biochemical properties of thioredoxins
h.</abstract><pub>Elsevier Masson SAS</pub><doi>10.1016/S0981-9428(03)00063-9</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-0699-9113</orcidid><orcidid>https://orcid.org/0000-0003-4975-8587</orcidid><orcidid>https://orcid.org/0000-0002-2036-7884</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0981-9428 |
| ispartof | Plant physiology and biochemistry, 2003-06, Vol.41 (6), p.629-635 |
| issn | 0981-9428 1873-2690 |
| language | eng |
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| source | Elsevier |
| subjects | Biochemistry, Molecular Biology CHEMICOPHYSICAL PROPERTIES COMPOSÉ ORGANOSOUFRÉ COMPUESTO ORGÁNICO DEL AZUFRE Life Sciences Medicin och hälsovetenskap MUTANT MUTANTES MUTANTS NUCLEOTIDE SEQUENCE ORGANOSULPHUR COMPOUNDS OXIDOREDUCTIONS OXIRREDUCIÓN OXYDORÉDUCTION POPULUS POTENCIAL REDOX POTENTIEL REDOX PROPIEDADES FISICOQUÍMICAS PROPRIÉTÉ PHYSICOCHIMIQUE PROTEINS PROTEÍNAS PROTÉINE RECOMBINACIÓN RECOMBINAISON Recombinant RECOMBINATION REDOX POTENTIAL Redox regulation SECUENCIA NUCLEOTÍDICA SÉQUENCE NUCLÉOTIDIQUE Thioredoxin h |
| title | Identification and characterization of a third thioredoxin h in poplar |
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