Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile.
Identifieur interne : 001183 ( Main/Exploration ); précédent : 001182; suivant : 001184Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile.
Auteurs : A. Jordan [Suède] ; F. Aslund ; E. Pontis ; P. Reichard ; A. HolmgrenSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1997.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Amorces ADN (MeSH), Cinétique (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (génétique), Escherichia coli (métabolisme), Glutarédoxines (MeSH), Oxidoreductases (MeSH), Phylogenèse (MeSH), Protéines (composition chimique), Protéines (métabolisme), Protéines Escherichia coli (MeSH), Protéines bactériennes (biosynthèse), Protéines bactériennes (composition chimique), Protéines bactériennes (métabolisme), Protéines recombinantes (biosynthèse), Protéines recombinantes (isolement et purification), Protéines recombinantes (métabolisme), Ribonucleotide reductases (métabolisme), Réaction de polymérisation en chaîne (MeSH), Salmonella typhimurium (génétique), Salmonella typhimurium (métabolisme), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme).
- MESH :
- biosynthèse : Protéines bactériennes, Protéines recombinantes.
- composition chimique : Protéines, Protéines bactériennes, Thiorédoxines.
- génétique : Escherichia coli, Salmonella typhimurium.
- isolement et purification : Protéines recombinantes.
- métabolisme : Escherichia coli, Protéines, Protéines bactériennes, Protéines recombinantes, Ribonucleotide reductases, Salmonella typhimurium, Thiorédoxines.
- Alignement de séquences, Amorces ADN, Cinétique, Clonage moléculaire, Données de séquences moléculaires, Glutarédoxines, Oxidoreductases, Phylogenèse, Protéines Escherichia coli, Réaction de polymérisation en chaîne, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacterial Proteins (biosynthesis), Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Cloning, Molecular (MeSH), DNA Primers (MeSH), Escherichia coli (genetics), Escherichia coli (metabolism), Escherichia coli Proteins (MeSH), Glutaredoxins (MeSH), Kinetics (MeSH), Molecular Sequence Data (MeSH), Oxidoreductases (MeSH), Phylogeny (MeSH), Polymerase Chain Reaction (MeSH), Proteins (chemistry), Proteins (metabolism), Recombinant Proteins (biosynthesis), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Ribonucleotide Reductases (metabolism), Salmonella typhimurium (genetics), Salmonella typhimurium (metabolism), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Thioredoxins (chemistry), Thioredoxins (metabolism).
- MESH :
- chemical , biosynthesis : Bacterial Proteins, Recombinant Proteins.
- chemical , chemistry : Bacterial Proteins, Proteins, Thioredoxins.
- chemical , isolation & purification : Recombinant Proteins.
- chemical , metabolism : Bacterial Proteins, Proteins, Recombinant Proteins, Ribonucleotide Reductases, Thioredoxins.
- genetics : Escherichia coli, Salmonella typhimurium.
- metabolism : Escherichia coli, Salmonella typhimurium.
- Amino Acid Sequence, Cloning, Molecular, DNA Primers, Escherichia coli Proteins, Glutaredoxins, Kinetics, Molecular Sequence Data, Oxidoreductases, Phylogeny, Polymerase Chain Reaction, Sequence Alignment, Sequence Homology, Amino Acid.
Abstract
Ribonucleotides are converted to deoxyribonucleotides by ribonucleotide reductases. Either thioredoxin or glutaredoxin is a required electron donor for class I and II enzymes. Glutaredoxins are reduced by glutathione, thioredoxins by thioredoxin reductase. Recently, a glutaredoxin-like protein, NrdH, was isolated as the functional electron donor for a NrdEF ribonucleotide reductase, a class Ib enzyme, from Lactococcus lactis. The absence of glutathione in this bacterium raised the question of the identity of the intracellular reductant for NrdH. Homologues of NrdH are present in the genomes of Escherichia coli and Salmonella typhimurium, upstream of the genes for the poorly transcribed nrdEF, separated from it by an open reading frame (nrdI) coding for a protein of unknown function. Overexpression of E. coli NrdH protein shows that it is a functional hydrogen donor with higher specificity for the class Ib (NrdEF) than for the class Ia (NrdAB) ribonucleotide reductase. Furthermore, this glutaredoxin-like enzyme is reduced by thioredoxin reductase and not by glutathione. We suggest that several uncharacterized glutaredoxin-like proteins present in the genomes of organisms lacking GSH, including archae, will also react with thioredoxin reductase and be related to the ancestors from which the GSH-dependent glutaredoxins have evolved by the acquisition of a GSH-binding site. We also show that NrdI, encoded by all nrdEF operons, has a stimulatory effect on ribonucleotide reduction.
DOI: 10.1074/jbc.272.29.18044
PubMed: 9218434
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Pontis</name></author><author><name sortKey="Reichard, P" sort="Reichard, P" uniqKey="Reichard P" first="P" last="Reichard">P. Reichard</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1997">1997</date><idno type="RBID">pubmed:9218434</idno><idno type="pmid">9218434</idno><idno type="doi">10.1074/jbc.272.29.18044</idno><idno type="wicri:Area/Main/Corpus">001167</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001167</idno><idno type="wicri:Area/Main/Curation">001167</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001167</idno><idno type="wicri:Area/Main/Exploration">001167</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile.</title><author><name sortKey="Jordan, A" sort="Jordan, A" uniqKey="Jordan A" first="A" last="Jordan">A. Jordan</name><affiliation wicri:level="1"><nlm:affiliation>Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm</wicri:regionArea><wicri:noRegion>S-171 77 Stockholm</wicri:noRegion></affiliation></author><author><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name></author><author><name sortKey="Pontis, E" sort="Pontis, E" uniqKey="Pontis E" first="E" last="Pontis">E. 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(biosynthesis)</term><term>Recombinant Proteins (isolation & purification)</term><term>Recombinant Proteins (metabolism)</term><term>Ribonucleotide Reductases (metabolism)</term><term>Salmonella typhimurium (genetics)</term><term>Salmonella typhimurium (metabolism)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Amorces ADN (MeSH)</term><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (génétique)</term><term>Escherichia coli (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Phylogenèse (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines (métabolisme)</term><term>Protéines Escherichia coli (MeSH)</term><term>Protéines bactériennes (biosynthèse)</term><term>Protéines bactériennes (composition chimique)</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines recombinantes (biosynthèse)</term><term>Protéines recombinantes (isolement et purification)</term><term>Protéines recombinantes (métabolisme)</term><term>Ribonucleotide reductases (métabolisme)</term><term>Réaction de polymérisation en chaîne (MeSH)</term><term>Salmonella typhimurium (génétique)</term><term>Salmonella typhimurium (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Bacterial Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial 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Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Amorces ADN</term><term>Cinétique</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Phylogenèse</term><term>Protéines Escherichia coli</term><term>Réaction de polymérisation en chaîne</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ribonucleotides are converted to deoxyribonucleotides by ribonucleotide reductases. Either thioredoxin or glutaredoxin is a required electron donor for class I and II enzymes. Glutaredoxins are reduced by glutathione, thioredoxins by thioredoxin reductase. Recently, a glutaredoxin-like protein, NrdH, was isolated as the functional electron donor for a NrdEF ribonucleotide reductase, a class Ib enzyme, from Lactococcus lactis. The absence of glutathione in this bacterium raised the question of the identity of the intracellular reductant for NrdH. Homologues of NrdH are present in the genomes of Escherichia coli and Salmonella typhimurium, upstream of the genes for the poorly transcribed nrdEF, separated from it by an open reading frame (nrdI) coding for a protein of unknown function. Overexpression of E. coli NrdH protein shows that it is a functional hydrogen donor with higher specificity for the class Ib (NrdEF) than for the class Ia (NrdAB) ribonucleotide reductase. Furthermore, this glutaredoxin-like enzyme is reduced by thioredoxin reductase and not by glutathione. We suggest that several uncharacterized glutaredoxin-like proteins present in the genomes of organisms lacking GSH, including archae, will also react with thioredoxin reductase and be related to the ancestors from which the GSH-dependent glutaredoxins have evolved by the acquisition of a GSH-binding site. We also show that NrdI, encoded by all nrdEF operons, has a stimulatory effect on ribonucleotide reduction.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9218434</PMID><DateCompleted><Year>1997</Year><Month>08</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>272</Volume><Issue>29</Issue><PubDate><Year>1997</Year><Month>Jul</Month><Day>18</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile.</ArticleTitle><Pagination><MedlinePgn>18044-50</MedlinePgn></Pagination><Abstract><AbstractText>Ribonucleotides are converted to deoxyribonucleotides by ribonucleotide reductases. Either thioredoxin or glutaredoxin is a required electron donor for class I and II enzymes. Glutaredoxins are reduced by glutathione, thioredoxins by thioredoxin reductase. Recently, a glutaredoxin-like protein, NrdH, was isolated as the functional electron donor for a NrdEF ribonucleotide reductase, a class Ib enzyme, from Lactococcus lactis. The absence of glutathione in this bacterium raised the question of the identity of the intracellular reductant for NrdH. Homologues of NrdH are present in the genomes of Escherichia coli and Salmonella typhimurium, upstream of the genes for the poorly transcribed nrdEF, separated from it by an open reading frame (nrdI) coding for a protein of unknown function. Overexpression of E. coli NrdH protein shows that it is a functional hydrogen donor with higher specificity for the class Ib (NrdEF) than for the class Ia (NrdAB) ribonucleotide reductase. Furthermore, this glutaredoxin-like enzyme is reduced by thioredoxin reductase and not by glutathione. We suggest that several uncharacterized glutaredoxin-like proteins present in the genomes of organisms lacking GSH, including archae, will also react with thioredoxin reductase and be related to the ancestors from which the GSH-dependent glutaredoxins have evolved by the acquisition of a GSH-binding site. We also show that NrdI, encoded by all nrdEF operons, has a stimulatory effect on ribonucleotide reduction.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jordan</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aslund</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Pontis</LastName><ForeName>E</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Reichard</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029968">Escherichia coli Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C107179">NrdH protein, E Coli</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.17.4.-</RegistryNumber><NameOfSubstance UI="D012264">Ribonucleotide Reductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029968" MajorTopicYN="Y">Escherichia coli Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016133" MajorTopicYN="N">Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012264" MajorTopicYN="N">Ribonucleotide Reductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012486" MajorTopicYN="N">Salmonella typhimurium</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>7</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>7</Month><Day>18</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>7</Month><Day>18</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9218434</ArticleId><ArticleId IdType="doi">10.1074/jbc.272.29.18044</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Pontis, E" sort="Pontis, E" uniqKey="Pontis E" first="E" last="Pontis">E. Pontis</name><name sortKey="Reichard, P" sort="Reichard, P" uniqKey="Reichard P" first="P" last="Reichard">P. Reichard</name></noCountry><country name="Suède"><noRegion><name sortKey="Jordan, A" sort="Jordan, A" uniqKey="Jordan A" first="A" last="Jordan">A. Jordan</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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