Isolation and characterization of an extended thioredoxin h from poplar.
Identifieur interne : 004571 ( Main/Exploration ); précédent : 004570; suivant : 004572Isolation and characterization of an extended thioredoxin h from poplar.
Auteurs : Eric Gelhaye [France] ; Nicolas Rouhier ; Pascal Laurent ; Pierre-Eric Sautière ; Francis Martin ; Jean-Pierre JacquotSource :
- Physiologia plantarum [ 1399-3054 ] ; 2002.
Abstract
A cDNA coding for a thioredoxin h has been isolated from a xylem/phloem poplar cDNA library by RACE-PCR. The nucleotide sequence called popTrx-h2 is homologous to other thioredoxins h isolated from plants but differs from the other thioredoxins h by presenting a 30 amino acid long N-terminus extension. A variant of this cDNA lacking the N-terminal extension was also generated by PCR. Both cDNAs have been introduced into an expression plasmid (pET-3d) and the recombinant proteins have been expressed to a high level and purified from Escherichia coli cells. Protein sequencing showed that a part of the N-terminal extension was cleaved in the E. coli cells, with the first 19 amino acids missing, suggesting the presence of a putative cleavage site in the N-terminal extension of popTrx-h2. Both recombinant proteins display unusual catalytic properties compared to other thioredoxins h characterized so far, i.e. a weak reduction by Arabidopsis thaliana NADPH-dependent thioredoxin reductase, and a weak activation of the chloroplastic NADP-malate dehydrogenase, a non-physiological target enzyme. Northern blot experiments indicate that the transcripts of popTrx-h2 are present in leaves and roots, albeit at a lower level compared to the earlier characterized popTrx-h1.
DOI: 10.1034/j.1399-3054.2002.1140202.x
PubMed: 11903963
Affiliations:
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Poincaré-Nancy I. Faculté des Sciences F-54506 Vandoeuvre, France UMR IaM 1136 INRA-Université H. Poincaré-Nancy I. Centre INRA de Nancy., F-54280 Champenoux, France Laboratoire d'Endocrinologie des Annélides UPRESA 8017. Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR IaM 1136 INRA-Université H. Poincaré-Nancy I. Faculté des Sciences F-54506 Vandoeuvre, France UMR IaM 1136 INRA-Université H. Poincaré-Nancy I. Centre INRA de Nancy., F-54280 Champenoux, France Laboratoire d'Endocrinologie des Annélides UPRESA 8017. Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Hauts-de-France</region><region type="old region" nuts="2">Nord-Pas-de-Calais</region><settlement type="city">Villeneuve d'Ascq</settlement></placeName></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author><author><name sortKey="Laurent, Pascal" sort="Laurent, Pascal" uniqKey="Laurent P" first="Pascal" last="Laurent">Pascal Laurent</name></author><author><name sortKey="Sautiere, Pierre Eric" sort="Sautiere, Pierre Eric" uniqKey="Sautiere P" first="Pierre-Eric" last="Sautière">Pierre-Eric Sautière</name></author><author><name sortKey="Martin, Francis" sort="Martin, Francis" uniqKey="Martin F" first="Francis" last="Martin">Francis Martin</name></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author></analytic><series><title level="j">Physiologia plantarum</title><idno type="eISSN">1399-3054</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A cDNA coding for a thioredoxin h has been isolated from a xylem/phloem poplar cDNA library by RACE-PCR. The nucleotide sequence called popTrx-h2 is homologous to other thioredoxins h isolated from plants but differs from the other thioredoxins h by presenting a 30 amino acid long N-terminus extension. A variant of this cDNA lacking the N-terminal extension was also generated by PCR. Both cDNAs have been introduced into an expression plasmid (pET-3d) and the recombinant proteins have been expressed to a high level and purified from Escherichia coli cells. Protein sequencing showed that a part of the N-terminal extension was cleaved in the E. coli cells, with the first 19 amino acids missing, suggesting the presence of a putative cleavage site in the N-terminal extension of popTrx-h2. Both recombinant proteins display unusual catalytic properties compared to other thioredoxins h characterized so far, i.e. a weak reduction by Arabidopsis thaliana NADPH-dependent thioredoxin reductase, and a weak activation of the chloroplastic NADP-malate dehydrogenase, a non-physiological target enzyme. Northern blot experiments indicate that the transcripts of popTrx-h2 are present in leaves and roots, albeit at a lower level compared to the earlier characterized popTrx-h1.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">11903963</PMID><DateRevised><Year>2019</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1399-3054</ISSN><JournalIssue CitedMedium="Internet"><Volume>114</Volume><Issue>2</Issue><PubDate><Year>2002</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Physiologia plantarum</Title><ISOAbbreviation>Physiol Plant</ISOAbbreviation></Journal><ArticleTitle>Isolation and characterization of an extended thioredoxin h from poplar.</ArticleTitle><Pagination><MedlinePgn>165-171</MedlinePgn></Pagination><Abstract><AbstractText>A cDNA coding for a thioredoxin h has been isolated from a xylem/phloem poplar cDNA library by RACE-PCR. The nucleotide sequence called popTrx-h2 is homologous to other thioredoxins h isolated from plants but differs from the other thioredoxins h by presenting a 30 amino acid long N-terminus extension. A variant of this cDNA lacking the N-terminal extension was also generated by PCR. Both cDNAs have been introduced into an expression plasmid (pET-3d) and the recombinant proteins have been expressed to a high level and purified from Escherichia coli cells. Protein sequencing showed that a part of the N-terminal extension was cleaved in the E. coli cells, with the first 19 amino acids missing, suggesting the presence of a putative cleavage site in the N-terminal extension of popTrx-h2. Both recombinant proteins display unusual catalytic properties compared to other thioredoxins h characterized so far, i.e. a weak reduction by Arabidopsis thaliana NADPH-dependent thioredoxin reductase, and a weak activation of the chloroplastic NADP-malate dehydrogenase, a non-physiological target enzyme. 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Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Laurent</LastName><ForeName>Pascal</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Sautière</LastName><ForeName>Pierre-Eric</ForeName><Initials>PE</Initials></Author><Author ValidYN="Y"><LastName>Martin</LastName><ForeName>Francis</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Denmark</Country><MedlineTA>Physiol Plant</MedlineTA><NlmUniqueID>1256322</NlmUniqueID><ISSNLinking>0031-9317</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>3</Month><Day>21</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>3</Month><Day>21</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>3</Month><Day>21</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11903963</ArticleId><ArticleId IdType="pii">ppl1140202</ArticleId><ArticleId IdType="doi">10.1034/j.1399-3054.2002.1140202.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Hauts-de-France</li><li>Nord-Pas-de-Calais</li></region><settlement><li>Villeneuve d'Ascq</li></settlement></list><tree><noCountry><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Laurent, Pascal" sort="Laurent, Pascal" uniqKey="Laurent P" first="Pascal" last="Laurent">Pascal Laurent</name><name sortKey="Martin, Francis" sort="Martin, Francis" uniqKey="Martin F" first="Francis" last="Martin">Francis Martin</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Sautiere, Pierre Eric" sort="Sautiere, Pierre Eric" uniqKey="Sautiere P" first="Pierre-Eric" last="Sautière">Pierre-Eric Sautière</name></noCountry><country name="France"><region name="Hauts-de-France"><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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