Loading…

Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana

Thioredoxins, by reducing disulfide bridges are one of the main participants that regulate cellular redox balance. In plants, the thioredoxin system is particularly complex. The most well-known thioredoxins are the chloroplastic ones, that participate in the regulation of enzymatic activities during...

Full description

Saved in:
Bibliographic Details
Published in:Photosynthesis research 2004-01, Vol.79 (3), p.295-304
Main Authors: Bréhélin, Claire, Laloi, Christophe, Setterdahl, Aaron T, Knaff, David B, Meyer, Yves
Format: Article
Language:English
Subjects:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c411t-681167a16ea9cced55062efcf2fa801f6a5de5be183470163161d2e1bddf11653
cites
container_end_page 304
container_issue 3
container_start_page 295
container_title Photosynthesis research
container_volume 79
creator Bréhélin, Claire
Laloi, Christophe
Setterdahl, Aaron T
Knaff, David B
Meyer, Yves
description Thioredoxins, by reducing disulfide bridges are one of the main participants that regulate cellular redox balance. In plants, the thioredoxin system is particularly complex. The most well-known thioredoxins are the chloroplastic ones, that participate in the regulation of enzymatic activities during the transition between light and dark phases. The mitochondrial system composed of NADPH-dependent thioredoxin reductase and type o thioredoxin has only recently been described. The type h thioredoxin group is better known. Yeast complementation experiments demonstrated that Arabidopsis thaliana thioredoxins h have divergent functions, at least in Saccharomyces cerevisiae. They have diverse affinities for different target proteins, most probably because of structural differences. However, plant thioredoxin h functions still have to be defined.
doi_str_mv 10.1023/B:PRES.0000017165.55488.ca
format article
fullrecord <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_02348775v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1859501247</sourcerecordid><originalsourceid>FETCH-LOGICAL-c411t-681167a16ea9cced55062efcf2fa801f6a5de5be183470163161d2e1bddf11653</originalsourceid><addsrcrecordid>eNp9kVtr3DAQhUVoSTZp_kIxeSgNxFuNZV2ct82SS2GhpW2gb2JWkomC19pKdmn-feTu0pQ-VC-Dhu_oaOYQcgZ0DrRiH64uP3-5_jqn0wEJgs85r5WaGzwgM-CSlZzK5hWZURCiVLzhR-Q4pceMKwHskByBYJWSjZiR78unIaTQeXNRbPwQzEPobfTYFcODD9HZ8Mv3qcDe_t0och3NgMmlIt8WEdfehm3yKVPYeezxDXndYpfc6b6ekPub62_Lu3L16fbjcrEqTQ0wlEIBCIkgHDbGOMs5FZVrTVu1qCi0Arl1fO1AsVrmeRgIsJWDtbVtVnJ2Qs5372ZfvY1-g_FJB_T6brHSUy9vrFZS8p-Q2fc7dhvDj9GlQW98Mq7rsHdhTBqmXVGoapnRd_9HpWoUFXUGz_4BH8MY-zyylpypRgg6GV_uIBNDStG1f34KVE-Z6is9ZapfMtW_M9UGs_jt3mFcb5x9ke5DZM_Tm54T</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>753896601</pqid></control><display><type>article</type><title>Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana</title><source>Springer Link</source><creator>Bréhélin, Claire ; Laloi, Christophe ; Setterdahl, Aaron T ; Knaff, David B ; Meyer, Yves</creator><creatorcontrib>Bréhélin, Claire ; Laloi, Christophe ; Setterdahl, Aaron T ; Knaff, David B ; Meyer, Yves</creatorcontrib><description>Thioredoxins, by reducing disulfide bridges are one of the main participants that regulate cellular redox balance. In plants, the thioredoxin system is particularly complex. The most well-known thioredoxins are the chloroplastic ones, that participate in the regulation of enzymatic activities during the transition between light and dark phases. The mitochondrial system composed of NADPH-dependent thioredoxin reductase and type o thioredoxin has only recently been described. The type h thioredoxin group is better known. Yeast complementation experiments demonstrated that Arabidopsis thaliana thioredoxins h have divergent functions, at least in Saccharomyces cerevisiae. They have diverse affinities for different target proteins, most probably because of structural differences. However, plant thioredoxin h functions still have to be defined.</description><identifier>ISSN: 0166-8595</identifier><identifier>EISSN: 1573-5079</identifier><identifier>DOI: 10.1023/B:PRES.0000017165.55488.ca</identifier><identifier>PMID: 16328796</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Arabidopsis thaliana ; Enzymes ; Life Sciences ; Mitochondria ; Photosynthesis ; Plant biology ; Saccharomyces cerevisiae ; Vegetal Biology</subject><ispartof>Photosynthesis research, 2004-01, Vol.79 (3), p.295-304</ispartof><rights>Kluwer Academic Publishers 2004</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c411t-681167a16ea9cced55062efcf2fa801f6a5de5be183470163161d2e1bddf11653</citedby><orcidid>0000-0002-1889-9582 ; 0000-0002-6576-5966</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16328796$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02348775$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Bréhélin, Claire</creatorcontrib><creatorcontrib>Laloi, Christophe</creatorcontrib><creatorcontrib>Setterdahl, Aaron T</creatorcontrib><creatorcontrib>Knaff, David B</creatorcontrib><creatorcontrib>Meyer, Yves</creatorcontrib><title>Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana</title><title>Photosynthesis research</title><addtitle>Photosynth Res</addtitle><description>Thioredoxins, by reducing disulfide bridges are one of the main participants that regulate cellular redox balance. In plants, the thioredoxin system is particularly complex. The most well-known thioredoxins are the chloroplastic ones, that participate in the regulation of enzymatic activities during the transition between light and dark phases. The mitochondrial system composed of NADPH-dependent thioredoxin reductase and type o thioredoxin has only recently been described. The type h thioredoxin group is better known. Yeast complementation experiments demonstrated that Arabidopsis thaliana thioredoxins h have divergent functions, at least in Saccharomyces cerevisiae. They have diverse affinities for different target proteins, most probably because of structural differences. However, plant thioredoxin h functions still have to be defined.</description><subject>Arabidopsis thaliana</subject><subject>Enzymes</subject><subject>Life Sciences</subject><subject>Mitochondria</subject><subject>Photosynthesis</subject><subject>Plant biology</subject><subject>Saccharomyces cerevisiae</subject><subject>Vegetal Biology</subject><issn>0166-8595</issn><issn>1573-5079</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNp9kVtr3DAQhUVoSTZp_kIxeSgNxFuNZV2ct82SS2GhpW2gb2JWkomC19pKdmn-feTu0pQ-VC-Dhu_oaOYQcgZ0DrRiH64uP3-5_jqn0wEJgs85r5WaGzwgM-CSlZzK5hWZURCiVLzhR-Q4pceMKwHskByBYJWSjZiR78unIaTQeXNRbPwQzEPobfTYFcODD9HZ8Mv3qcDe_t0och3NgMmlIt8WEdfehm3yKVPYeezxDXndYpfc6b6ekPub62_Lu3L16fbjcrEqTQ0wlEIBCIkgHDbGOMs5FZVrTVu1qCi0Arl1fO1AsVrmeRgIsJWDtbVtVnJ2Qs5372ZfvY1-g_FJB_T6brHSUy9vrFZS8p-Q2fc7dhvDj9GlQW98Mq7rsHdhTBqmXVGoapnRd_9HpWoUFXUGz_4BH8MY-zyylpypRgg6GV_uIBNDStG1f34KVE-Z6is9ZapfMtW_M9UGs_jt3mFcb5x9ke5DZM_Tm54T</recordid><startdate>20040101</startdate><enddate>20040101</enddate><creator>Bréhélin, Claire</creator><creator>Laloi, Christophe</creator><creator>Setterdahl, Aaron T</creator><creator>Knaff, David B</creator><creator>Meyer, Yves</creator><general>Springer Nature B.V</general><general>Springer Verlag</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QP</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-1889-9582</orcidid><orcidid>https://orcid.org/0000-0002-6576-5966</orcidid></search><sort><creationdate>20040101</creationdate><title>Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana</title><author>Bréhélin, Claire ; Laloi, Christophe ; Setterdahl, Aaron T ; Knaff, David B ; Meyer, Yves</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-681167a16ea9cced55062efcf2fa801f6a5de5be183470163161d2e1bddf11653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Arabidopsis thaliana</topic><topic>Enzymes</topic><topic>Life Sciences</topic><topic>Mitochondria</topic><topic>Photosynthesis</topic><topic>Plant biology</topic><topic>Saccharomyces cerevisiae</topic><topic>Vegetal Biology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bréhélin, Claire</creatorcontrib><creatorcontrib>Laloi, Christophe</creatorcontrib><creatorcontrib>Setterdahl, Aaron T</creatorcontrib><creatorcontrib>Knaff, David B</creatorcontrib><creatorcontrib>Meyer, Yves</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Health &amp; Medical Collection (Proquest)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database (ProQuest)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Photosynthesis research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bréhélin, Claire</au><au>Laloi, Christophe</au><au>Setterdahl, Aaron T</au><au>Knaff, David B</au><au>Meyer, Yves</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana</atitle><jtitle>Photosynthesis research</jtitle><addtitle>Photosynth Res</addtitle><date>2004-01-01</date><risdate>2004</risdate><volume>79</volume><issue>3</issue><spage>295</spage><epage>304</epage><pages>295-304</pages><issn>0166-8595</issn><eissn>1573-5079</eissn><abstract>Thioredoxins, by reducing disulfide bridges are one of the main participants that regulate cellular redox balance. In plants, the thioredoxin system is particularly complex. The most well-known thioredoxins are the chloroplastic ones, that participate in the regulation of enzymatic activities during the transition between light and dark phases. The mitochondrial system composed of NADPH-dependent thioredoxin reductase and type o thioredoxin has only recently been described. The type h thioredoxin group is better known. Yeast complementation experiments demonstrated that Arabidopsis thaliana thioredoxins h have divergent functions, at least in Saccharomyces cerevisiae. They have diverse affinities for different target proteins, most probably because of structural differences. However, plant thioredoxin h functions still have to be defined.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>16328796</pmid><doi>10.1023/B:PRES.0000017165.55488.ca</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-1889-9582</orcidid><orcidid>https://orcid.org/0000-0002-6576-5966</orcidid></addata></record>
fulltext fulltext
identifier ISSN: 0166-8595
ispartof Photosynthesis research, 2004-01, Vol.79 (3), p.295-304
issn 0166-8595
1573-5079
language eng
recordid cdi_hal_primary_oai_HAL_hal_02348775v1
source Springer Link
subjects Arabidopsis thaliana
Enzymes
Life Sciences
Mitochondria
Photosynthesis
Plant biology
Saccharomyces cerevisiae
Vegetal Biology
title Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-30T21%3A57%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cytosolic,%20mitochondrial%20thioredoxins%20and%20thioredoxin%20reductases%20in%20Arabidopsis%20thaliana&rft.jtitle=Photosynthesis%20research&rft.au=Br%C3%A9h%C3%A9lin,%20Claire&rft.date=2004-01-01&rft.volume=79&rft.issue=3&rft.spage=295&rft.epage=304&rft.pages=295-304&rft.issn=0166-8595&rft.eissn=1573-5079&rft_id=info:doi/10.1023/B:PRES.0000017165.55488.ca&rft_dat=%3Cproquest_hal_p%3E1859501247%3C/proquest_hal_p%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c411t-681167a16ea9cced55062efcf2fa801f6a5de5be183470163161d2e1bddf11653%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=753896601&rft_id=info:pmid/16328796&rfr_iscdi=true