Null thioredoxin and glutaredoxin Escherichia coli K-12 mutants have no enhanced sensitivity to mutagens due to a new GSH-dependent hydrogen donor and high increases in ribonucleotide reductase activity.
Identifieur interne : 001247 ( Main/Exploration ); précédent : 001246; suivant : 001248Null thioredoxin and glutaredoxin Escherichia coli K-12 mutants have no enhanced sensitivity to mutagens due to a new GSH-dependent hydrogen donor and high increases in ribonucleotide reductase activity.
Auteurs : A. Miranda-Vizuete [Espagne] ; E. Martinez-Galisteo ; F. Aslund ; J. Lopez-Barea ; C. Pueyo ; A. HolmgrenSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1994.
Descripteurs français
- KwdFr :
- Escherichia coli (effets des médicaments et des substances chimiques), Escherichia coli (génétique), Escherichia coli (métabolisme), Glutarédoxines (MeSH), Glutathion (métabolisme), Gènes bactériens (MeSH), Génotype (MeSH), Mutagenèse (MeSH), Mutagènes (toxicité), Oxidoreductases (MeSH), Protéines (génétique), Protéines bactériennes (génétique), Ribonucleotide reductases (métabolisme), Spécificité d'espèce (MeSH), Tests de mutagénicité (MeSH), Thiorédoxines (génétique).
- MESH :
- effets des médicaments et des substances chimiques : Escherichia coli.
- génétique : Escherichia coli, Protéines, Protéines bactériennes, Thiorédoxines.
- métabolisme : Escherichia coli, Glutathion, Ribonucleotide reductases.
- toxicité : Mutagènes.
- Glutarédoxines, Gènes bactériens, Génotype, Mutagenèse, Oxidoreductases, Spécificité d'espèce, Tests de mutagénicité.
English descriptors
- KwdEn :
- Bacterial Proteins (genetics), Escherichia coli (drug effects), Escherichia coli (genetics), Escherichia coli (metabolism), Genes, Bacterial (MeSH), Genotype (MeSH), Glutaredoxins (MeSH), Glutathione (metabolism), Mutagenesis (MeSH), Mutagenicity Tests (MeSH), Mutagens (toxicity), Oxidoreductases (MeSH), Proteins (genetics), Ribonucleotide Reductases (metabolism), Species Specificity (MeSH), Thioredoxins (genetics).
- MESH :
- chemical , genetics : Bacterial Proteins, Proteins, Thioredoxins.
- drug effects : Escherichia coli.
- genetics : Escherichia coli.
- metabolism : Escherichia coli, Glutathione, Ribonucleotide Reductases.
- chemical , toxicity : Mutagens.
- Genes, Bacterial, Genotype, Glutaredoxins, Mutagenesis, Mutagenicity Tests, Oxidoreductases, Species Specificity.
Abstract
This work investigates whether a mutator phenotype is associated to the simultaneous deficiency in thioredoxin and glutaredoxin, the two known hydrogen donors of ribonucleotide reductase. To this end, new Escherichia coli K-12 strains carrying delta trxA and/or grx::kan null mutations were constructed to monitor mutagenesis by selecting forward mutations to L-arabinose resistance. Highly sensitive and specific enzyme-linked immunoassays were developed to confirm that trx-grx- cells lacked thioredoxin and glutaredoxin. A number of remarkable properties were observed in the newly constructed thioredoxin- and glutaredoxin-deficient bacteria compared with the wild type cells. Thus, they (i) grew on minimal medium plates, suggesting that the presence of thioredoxin and glutaredoxin may not be absolutely essential for sulfate reduction; (ii) showed normal mutagenic sensitivities toward a wide variety of DNA-damaging agents, as compared with wild type cells and trx- or grx- single mutants; (iii) displayed 14% of GSH-dependent and 30% of NADPH-dependent ribonucleotide reduction capacity with CDP as substrate in the presence or the absence of exogenous ribonucleotide reductase, respectively; and (iv) showed very high levels of ribonucleotide reductase activity, which was increased from 19- to 23-fold. The existence of a new glutathione-dependent hydrogen donor for ribonucleotide reductase and the high activity levels of this enzyme in trx-grx- defective cells could explain that thioredoxin and the first discovered glutaredoxin are not essential for deoxyribonucleotide synthesis, even under mutagenic stress.
PubMed: 8206982
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Martinez-Galisteo</name></author><author><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name></author><author><name sortKey="Lopez Barea, J" sort="Lopez Barea, J" uniqKey="Lopez Barea J" first="J" last="Lopez-Barea">J. Lopez-Barea</name></author><author><name sortKey="Pueyo, C" sort="Pueyo, C" uniqKey="Pueyo C" first="C" last="Pueyo">C. Pueyo</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="1994">1994</date><idno type="RBID">pubmed:8206982</idno><idno type="pmid">8206982</idno><idno type="wicri:Area/Main/Corpus">001243</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001243</idno><idno type="wicri:Area/Main/Curation">001243</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001243</idno><idno type="wicri:Area/Main/Exploration">001243</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Null thioredoxin and glutaredoxin Escherichia coli K-12 mutants have no enhanced sensitivity to mutagens due to a new GSH-dependent hydrogen donor and high increases in ribonucleotide reductase activity.</title><author><name sortKey="Miranda Vizuete, A" sort="Miranda Vizuete, A" uniqKey="Miranda Vizuete A" first="A" last="Miranda-Vizuete">A. Miranda-Vizuete</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Genética, Universidad de Córdoba, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Genética, Universidad de Córdoba</wicri:regionArea><wicri:noRegion>Universidad de Córdoba</wicri:noRegion></affiliation></author><author><name sortKey="Martinez Galisteo, E" sort="Martinez Galisteo, E" uniqKey="Martinez Galisteo E" first="E" last="Martinez-Galisteo">E. Martinez-Galisteo</name></author><author><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name></author><author><name sortKey="Lopez Barea, J" sort="Lopez Barea, J" uniqKey="Lopez Barea J" first="J" last="Lopez-Barea">J. Lopez-Barea</name></author><author><name sortKey="Pueyo, C" sort="Pueyo, C" uniqKey="Pueyo C" first="C" last="Pueyo">C. Pueyo</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (genetics)</term><term>Escherichia coli (drug effects)</term><term>Escherichia coli (genetics)</term><term>Escherichia coli (metabolism)</term><term>Genes, Bacterial (MeSH)</term><term>Genotype (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (metabolism)</term><term>Mutagenesis (MeSH)</term><term>Mutagenicity Tests (MeSH)</term><term>Mutagens (toxicity)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (genetics)</term><term>Ribonucleotide Reductases (metabolism)</term><term>Species Specificity (MeSH)</term><term>Thioredoxins (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Escherichia coli (effets des médicaments et des substances chimiques)</term><term>Escherichia coli (génétique)</term><term>Escherichia coli (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (métabolisme)</term><term>Gènes bactériens (MeSH)</term><term>Génotype (MeSH)</term><term>Mutagenèse (MeSH)</term><term>Mutagènes (toxicité)</term><term>Oxidoreductases (MeSH)</term><term>Protéines (génétique)</term><term>Protéines bactériennes (génétique)</term><term>Ribonucleotide reductases (métabolisme)</term><term>Spécificité d'espèce (MeSH)</term><term>Tests de mutagénicité (MeSH)</term><term>Thiorédoxines (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Protéines</term><term>Protéines bactériennes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Glutathione</term><term>Ribonucleotide Reductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term><term>Glutathion</term><term>Ribonucleotide reductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Mutagens</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Mutagènes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Genes, Bacterial</term><term>Genotype</term><term>Glutaredoxins</term><term>Mutagenesis</term><term>Mutagenicity Tests</term><term>Oxidoreductases</term><term>Species Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Glutarédoxines</term><term>Gènes bactériens</term><term>Génotype</term><term>Mutagenèse</term><term>Oxidoreductases</term><term>Spécificité d'espèce</term><term>Tests de mutagénicité</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">This work investigates whether a mutator phenotype is associated to the simultaneous deficiency in thioredoxin and glutaredoxin, the two known hydrogen donors of ribonucleotide reductase. To this end, new Escherichia coli K-12 strains carrying delta trxA and/or grx::kan null mutations were constructed to monitor mutagenesis by selecting forward mutations to L-arabinose resistance. Highly sensitive and specific enzyme-linked immunoassays were developed to confirm that trx-grx- cells lacked thioredoxin and glutaredoxin. A number of remarkable properties were observed in the newly constructed thioredoxin- and glutaredoxin-deficient bacteria compared with the wild type cells. Thus, they (i) grew on minimal medium plates, suggesting that the presence of thioredoxin and glutaredoxin may not be absolutely essential for sulfate reduction; (ii) showed normal mutagenic sensitivities toward a wide variety of DNA-damaging agents, as compared with wild type cells and trx- or grx- single mutants; (iii) displayed 14% of GSH-dependent and 30% of NADPH-dependent ribonucleotide reduction capacity with CDP as substrate in the presence or the absence of exogenous ribonucleotide reductase, respectively; and (iv) showed very high levels of ribonucleotide reductase activity, which was increased from 19- to 23-fold. The existence of a new glutathione-dependent hydrogen donor for ribonucleotide reductase and the high activity levels of this enzyme in trx-grx- defective cells could explain that thioredoxin and the first discovered glutaredoxin are not essential for deoxyribonucleotide synthesis, even under mutagenic stress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8206982</PMID><DateCompleted><Year>1994</Year><Month>07</Month><Day>14</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>269</Volume><Issue>24</Issue><PubDate><Year>1994</Year><Month>Jun</Month><Day>17</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Null thioredoxin and glutaredoxin Escherichia coli K-12 mutants have no enhanced sensitivity to mutagens due to a new GSH-dependent hydrogen donor and high increases in ribonucleotide reductase activity.</ArticleTitle><Pagination><MedlinePgn>16631-7</MedlinePgn></Pagination><Abstract><AbstractText>This work investigates whether a mutator phenotype is associated to the simultaneous deficiency in thioredoxin and glutaredoxin, the two known hydrogen donors of ribonucleotide reductase. To this end, new Escherichia coli K-12 strains carrying delta trxA and/or grx::kan null mutations were constructed to monitor mutagenesis by selecting forward mutations to L-arabinose resistance. Highly sensitive and specific enzyme-linked immunoassays were developed to confirm that trx-grx- cells lacked thioredoxin and glutaredoxin. A number of remarkable properties were observed in the newly constructed thioredoxin- and glutaredoxin-deficient bacteria compared with the wild type cells. Thus, they (i) grew on minimal medium plates, suggesting that the presence of thioredoxin and glutaredoxin may not be absolutely essential for sulfate reduction; (ii) showed normal mutagenic sensitivities toward a wide variety of DNA-damaging agents, as compared with wild type cells and trx- or grx- single mutants; (iii) displayed 14% of GSH-dependent and 30% of NADPH-dependent ribonucleotide reduction capacity with CDP as substrate in the presence or the absence of exogenous ribonucleotide reductase, respectively; and (iv) showed very high levels of ribonucleotide reductase activity, which was increased from 19- to 23-fold. The existence of a new glutathione-dependent hydrogen donor for ribonucleotide reductase and the high activity levels of this enzyme in trx-grx- defective cells could explain that thioredoxin and the first discovered glutaredoxin are not essential for deoxyribonucleotide synthesis, even under mutagenic stress.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Miranda-Vizuete</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Departamento de Genética, Universidad de Córdoba, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martinez-Galisteo</LastName><ForeName>E</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Aslund</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Lopez-Barea</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Pueyo</LastName><ForeName>C</ForeName><Initials>C</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="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009153">Mutagens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">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><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><GeneSymbolList><GeneSymbol>grx</GeneSymbol><GeneSymbol>kan</GeneSymbol><GeneSymbol>trx</GeneSymbol><GeneSymbol>trxA</GeneSymbol></GeneSymbolList><MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005798" MajorTopicYN="N">Genes, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005838" MajorTopicYN="N">Genotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016296" MajorTopicYN="N">Mutagenesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009152" MajorTopicYN="N">Mutagenicity Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009153" MajorTopicYN="N">Mutagens</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012264" MajorTopicYN="N">Ribonucleotide Reductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013045" MajorTopicYN="N">Species Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>6</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1994</Year><Month>6</Month><Day>17</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>6</Month><Day>17</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8206982</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</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="Lopez Barea, J" sort="Lopez Barea, J" uniqKey="Lopez Barea J" first="J" last="Lopez-Barea">J. Lopez-Barea</name><name sortKey="Martinez Galisteo, E" sort="Martinez Galisteo, E" uniqKey="Martinez Galisteo E" first="E" last="Martinez-Galisteo">E. Martinez-Galisteo</name><name sortKey="Pueyo, C" sort="Pueyo, C" uniqKey="Pueyo C" first="C" last="Pueyo">C. Pueyo</name></noCountry><country name="Espagne"><noRegion><name sortKey="Miranda Vizuete, A" sort="Miranda Vizuete, A" uniqKey="Miranda Vizuete A" first="A" last="Miranda-Vizuete">A. Miranda-Vizuete</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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