A second class I ribonucleotide reductase in Enterobacteriaceae: characterization of the Salmonella typhimurium enzyme.
Identifieur interne : 001255 ( Main/Exploration ); précédent : 001254; suivant : 001256A second class I ribonucleotide reductase in Enterobacteriaceae: characterization of the Salmonella typhimurium enzyme.
Auteurs : A. Jordan [Suède] ; E. Pontis ; M. Atta ; M. Krook ; I. Gibert ; J. Barbé ; P. ReichardSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 1994.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Cytidine diphosphate (métabolisme), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Gènes bactériens (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (pharmacologie), Protéines bactériennes (isolement et purification), Ribonucleotide reductases (classification), Ribonucleotide reductases (génétique), Ribonucleotide reductases (métabolisme), Régulation allostérique (MeSH), Salmonella typhimurium (enzymologie), Spectroscopie de résonance de spin électronique (MeSH), Séquence d'acides aminés (MeSH), Test de complémentation (MeSH), Thiorédoxines (pharmacologie).
- MESH :
- classification : Ribonucleotide reductases.
- enzymologie : Salmonella typhimurium.
- génétique : Ribonucleotide reductases.
- isolement et purification : Protéines bactériennes.
- métabolisme : Cytidine diphosphate, Ribonucleotide reductases.
- pharmacologie : Protéines, Thiorédoxines.
- Catalyse, Données de séquences moléculaires, Glutarédoxines, Gènes bactériens, Oxidoreductases, Oxydoréduction, Régulation allostérique, Spectroscopie de résonance de spin électronique, Séquence d'acides aminés, Test de complémentation.
English descriptors
- KwdEn :
- Allosteric Regulation (MeSH), Amino Acid Sequence (MeSH), Bacterial Proteins (isolation & purification), Catalysis (MeSH), Cytidine Diphosphate (metabolism), Electron Spin Resonance Spectroscopy (MeSH), Genes, Bacterial (MeSH), Genetic Complementation Test (MeSH), Glutaredoxins (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Proteins (pharmacology), Ribonucleotide Reductases (classification), Ribonucleotide Reductases (genetics), Ribonucleotide Reductases (metabolism), Salmonella typhimurium (enzymology), Thioredoxins (pharmacology).
- MESH :
- chemical , classification : Ribonucleotide Reductases.
- chemical , genetics : Ribonucleotide Reductases.
- chemical , isolation & purification : Bacterial Proteins.
- chemical , metabolism : Cytidine Diphosphate, Ribonucleotide Reductases.
- chemical , pharmacology : Proteins, Thioredoxins.
- enzymology : Salmonella typhimurium.
- Allosteric Regulation, Amino Acid Sequence, Catalysis, Electron Spin Resonance Spectroscopy, Genes, Bacterial, Genetic Complementation Test, Glutaredoxins, Molecular Sequence Data, Oxidation-Reduction, Oxidoreductases.
Abstract
The nrdA and nrdB genes of Escherichia coli and Salmonella typhimurium encode the R1 and R2 proteins that together form an active class I ribonucleotide reductase. Both organisms contain two additional chromosomal genes, nrdE and nrdF, whose corresponding protein sequences show some homology to the products of the genes nrdA and nrdB. When present on a plasmid, nrdE and nrdF together complement mutations in nrdA or nrdB. We have now obtained in nearly homogeneous form the two proteins encoded by the S. typhimurium nrdE and nrdF genes (R1E and R2F). They correspond to the R1 and R2 proteins. Each protein is a homodimer. Together they catalyze the reduction of CDP to dCDP, using dithiothreitol or reduced glutaredoxin, but not thioredoxin, as an electron donor. CDP reduction is strongly stimulated by low concentrations of dATP, presumably acting as an allosteric effector. Protein R2F contains an antiferromagnetically coupled dinuclear iron center and a tyrosyl free radical. The E. coli and S. typhimurium chromosome thus have maintained the information for a potentially active additional class I ribonucleotide reductase, whose role in vivo is as yet unknown. The allosteric regulation of this enzyme differs from that of the normally expressed reductase.
DOI: 10.1073/pnas.91.26.12892
PubMed: 7809142
PubMed Central: PMC45546
Affiliations:
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Jordan</name><affiliation wicri:level="3"><nlm:affiliation>Department of Biochemistry I, Medical Nobel Institute, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Biochemistry I, Medical Nobel Institute, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Pontis, E" sort="Pontis, E" uniqKey="Pontis E" first="E" last="Pontis">E. Pontis</name></author><author><name sortKey="Atta, M" sort="Atta, M" uniqKey="Atta M" first="M" last="Atta">M. Atta</name></author><author><name sortKey="Krook, M" sort="Krook, M" uniqKey="Krook M" first="M" last="Krook">M. Krook</name></author><author><name sortKey="Gibert, I" sort="Gibert, I" uniqKey="Gibert I" first="I" last="Gibert">I. Gibert</name></author><author><name sortKey="Barbe, J" sort="Barbe, J" uniqKey="Barbe J" first="J" last="Barbé">J. 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Reichard</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allosteric Regulation (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Bacterial Proteins (isolation & purification)</term><term>Catalysis (MeSH)</term><term>Cytidine Diphosphate (metabolism)</term><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Genes, Bacterial (MeSH)</term><term>Genetic Complementation Test (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (pharmacology)</term><term>Ribonucleotide Reductases (classification)</term><term>Ribonucleotide Reductases (genetics)</term><term>Ribonucleotide Reductases (metabolism)</term><term>Salmonella typhimurium (enzymology)</term><term>Thioredoxins (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse (MeSH)</term><term>Cytidine diphosphate (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Gènes bactériens (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines (pharmacologie)</term><term>Protéines bactériennes (isolement et purification)</term><term>Ribonucleotide reductases (classification)</term><term>Ribonucleotide reductases (génétique)</term><term>Ribonucleotide reductases (métabolisme)</term><term>Régulation allostérique (MeSH)</term><term>Salmonella typhimurium (enzymologie)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Test de complémentation (MeSH)</term><term>Thiorédoxines (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Ribonucleotide Reductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Ribonucleotide Reductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Bacterial Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytidine Diphosphate</term><term>Ribonucleotide Reductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="fr"><term>Ribonucleotide reductases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Salmonella typhimurium</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Salmonella typhimurium</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ribonucleotide reductases</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytidine diphosphate</term><term>Ribonucleotide reductases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Protéines</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Allosteric Regulation</term><term>Amino Acid Sequence</term><term>Catalysis</term><term>Electron Spin Resonance Spectroscopy</term><term>Genes, Bacterial</term><term>Genetic Complementation Test</term><term>Glutaredoxins</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Gènes bactériens</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Régulation allostérique</term><term>Spectroscopie de résonance de spin électronique</term><term>Séquence d'acides aminés</term><term>Test de complémentation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The nrdA and nrdB genes of Escherichia coli and Salmonella typhimurium encode the R1 and R2 proteins that together form an active class I ribonucleotide reductase. Both organisms contain two additional chromosomal genes, nrdE and nrdF, whose corresponding protein sequences show some homology to the products of the genes nrdA and nrdB. When present on a plasmid, nrdE and nrdF together complement mutations in nrdA or nrdB. We have now obtained in nearly homogeneous form the two proteins encoded by the S. typhimurium nrdE and nrdF genes (R1E and R2F). They correspond to the R1 and R2 proteins. Each protein is a homodimer. Together they catalyze the reduction of CDP to dCDP, using dithiothreitol or reduced glutaredoxin, but not thioredoxin, as an electron donor. CDP reduction is strongly stimulated by low concentrations of dATP, presumably acting as an allosteric effector. Protein R2F contains an antiferromagnetically coupled dinuclear iron center and a tyrosyl free radical. The E. coli and S. typhimurium chromosome thus have maintained the information for a potentially active additional class I ribonucleotide reductase, whose role in vivo is as yet unknown. The allosteric regulation of this enzyme differs from that of the normally expressed reductase.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7809142</PMID><DateCompleted><Year>1995</Year><Month>02</Month><Day>02</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>91</Volume><Issue>26</Issue><PubDate><Year>1994</Year><Month>Dec</Month><Day>20</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>A second class I ribonucleotide reductase in Enterobacteriaceae: characterization of the Salmonella typhimurium enzyme.</ArticleTitle><Pagination><MedlinePgn>12892-6</MedlinePgn></Pagination><Abstract><AbstractText>The nrdA and nrdB genes of Escherichia coli and Salmonella typhimurium encode the R1 and R2 proteins that together form an active class I ribonucleotide reductase. Both organisms contain two additional chromosomal genes, nrdE and nrdF, whose corresponding protein sequences show some homology to the products of the genes nrdA and nrdB. When present on a plasmid, nrdE and nrdF together complement mutations in nrdA or nrdB. We have now obtained in nearly homogeneous form the two proteins encoded by the S. typhimurium nrdE and nrdF genes (R1E and R2F). They correspond to the R1 and R2 proteins. Each protein is a homodimer. Together they catalyze the reduction of CDP to dCDP, using dithiothreitol or reduced glutaredoxin, but not thioredoxin, as an electron donor. CDP reduction is strongly stimulated by low concentrations of dATP, presumably acting as an allosteric effector. Protein R2F contains an antiferromagnetically coupled dinuclear iron center and a tyrosyl free radical. The E. coli and S. typhimurium chromosome thus have maintained the information for a potentially active additional class I ribonucleotide reductase, whose role in vivo is as yet unknown. The allosteric regulation of this enzyme differs from that of the normally expressed reductase.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jordan</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biochemistry I, Medical Nobel Institute, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pontis</LastName><ForeName>E</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Atta</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Krook</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Gibert</LastName><ForeName>I</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Barbé</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Reichard</LastName><ForeName>P</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><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>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</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="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>63-38-7</RegistryNumber><NameOfSubstance UI="D003565">Cytidine Diphosphate</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><GeneSymbolList><GeneSymbol>nrdA</GeneSymbol><GeneSymbol>nrdB</GeneSymbol><GeneSymbol>nrdE</GeneSymbol><GeneSymbol>nrdF</GeneSymbol></GeneSymbolList><MeshHeadingList><MeshHeading><DescriptorName UI="D000494" MajorTopicYN="N">Allosteric Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003565" MajorTopicYN="N">Cytidine Diphosphate</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005798" MajorTopicYN="Y">Genes, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005816" MajorTopicYN="N">Genetic Complementation Test</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012264" MajorTopicYN="N">Ribonucleotide Reductases</DescriptorName><QualifierName UI="Q000145" MajorTopicYN="Y">classification</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012486" MajorTopicYN="N">Salmonella typhimurium</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000494" 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IdType="pubmed">7937896</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1972 Aug 4;28(4):492-6</Citation><ArticleIdList><ArticleId IdType="pubmed">5081610</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1972 Nov 25;247(22):7276-81</Citation><ArticleIdList><ArticleId IdType="pubmed">4565081</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1978;51:227-37</Citation><ArticleIdList><ArticleId IdType="pubmed">357894</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1980 Jul 25;255(14):6706-12</Citation><ArticleIdList><ArticleId IdType="pubmed">6248531</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1986 Aug;5(8):2037-40</Citation><ArticleIdList><ArticleId IdType="pubmed">3019680</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1987 Jan;169(1):19-25</Citation><ArticleIdList><ArticleId IdType="pubmed">3098730</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1987 Nov;169(11):5087-94</Citation><ArticleIdList><ArticleId IdType="pubmed">3312165</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Microbiol. 1988;149(4):344-9</Citation><ArticleIdList><ArticleId IdType="pubmed">2833197</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1989 Aug 25;264(24):13963-6</Citation><ArticleIdList><ArticleId IdType="pubmed">2668278</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 1990 Sep 11;18(17):5315-6</Citation><ArticleIdList><ArticleId IdType="pubmed">2402474</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Enzymol Relat Areas Mol Biol. 1992;65:147-83</Citation><ArticleIdList><ArticleId IdType="pubmed">1570768</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1992 Dec 15;267(35):25541-7</Citation><ArticleIdList><ArticleId IdType="pubmed">1460049</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1993 Jun 18;260(5115):1773-7</Citation><ArticleIdList><ArticleId IdType="pubmed">8511586</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1994 Jun;176(11):3420-7</Citation><ArticleIdList><ArticleId IdType="pubmed">8195103</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat New Biol. 1972 Jul 19;238(81):69-71</Citation><ArticleIdList><ArticleId IdType="pubmed">4558262</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><noCountry><name sortKey="Atta, M" sort="Atta, M" uniqKey="Atta M" first="M" last="Atta">M. Atta</name><name sortKey="Barbe, J" sort="Barbe, J" uniqKey="Barbe J" first="J" last="Barbé">J. Barbé</name><name sortKey="Gibert, I" sort="Gibert, I" uniqKey="Gibert I" first="I" last="Gibert">I. Gibert</name><name sortKey="Krook, M" sort="Krook, M" uniqKey="Krook M" first="M" last="Krook">M. Krook</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"><region name="Svealand"><name sortKey="Jordan, A" sort="Jordan, A" uniqKey="Jordan A" first="A" last="Jordan">A. Jordan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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