Visualization of ribonucleotide reductase catalytic oxidation establishes thioredoxins as its major reductants in yeast.
Identifieur interne : 000C38 ( Main/Exploration ); précédent : 000C37; suivant : 000C39Visualization of ribonucleotide reductase catalytic oxidation establishes thioredoxins as its major reductants in yeast.
Auteurs : Sylvie Camier [France] ; Emilie Ma ; Christophe Leroy ; Alain Pruvost ; Michel Toledano ; Marie-Claude Marsolier-KergoatSource :
- Free radical biology & medicine [ 0891-5849 ] ; 2007.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Saccharomyces cerevisiae.
- métabolisme : Ribonucleotide reductases, Saccharomyces cerevisiae, Thiorédoxines.
- Catalyse, Oxydoréduction, Plasmides.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Ribonucleotide Reductases, Thioredoxins.
- enzymology : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Catalysis, Oxidation-Reduction, Plasmids.
Abstract
Thioredoxins and/or glutaredoxins assist ribonucleotide reductase, and other such enzymes that require disulfide bond reduction during their catalytic cycle. In Saccharomyces cerevisiae, the presence of either pathway is essential but which of these pathways operates in ribonucleotide reductase reduction and how this function contributes to the pathways' essential nature have not been definitively established. We have identified two in vivo redox forms of the S. cerevisiae ribonucleotide reductase R1 subunit, which correspond to catalytically reduced or oxidized enzymes. Cells lacking thioredoxins, which exhibit an elongated S phase, accumulate R1 in its oxidized form and also contain significantly decreased deoxyribonucleotide levels during the S phase. Overexpressing R1 in these cells increases both the amount of the R1 reduced form and the concentrations of deoxyribonucleotides and accelerates DNA replication. These results establish thioredoxins as the major RNR reducing system in yeast and indicate that impaired RNR reduction accounts for the S phase defects of thioredoxin-deficient cells.
DOI: 10.1016/j.freeradbiomed.2006.12.027
PubMed: 17349928
Affiliations:
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xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Ribonucleotide reductases</term><term>Saccharomyces cerevisiae</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Oxidation-Reduction</term><term>Plasmids</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Oxydoréduction</term><term>Plasmides</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thioredoxins and/or glutaredoxins assist ribonucleotide reductase, and other such enzymes that require disulfide bond reduction during their catalytic cycle. In Saccharomyces cerevisiae, the presence of either pathway is essential but which of these pathways operates in ribonucleotide reductase reduction and how this function contributes to the pathways' essential nature have not been definitively established. We have identified two in vivo redox forms of the S. cerevisiae ribonucleotide reductase R1 subunit, which correspond to catalytically reduced or oxidized enzymes. Cells lacking thioredoxins, which exhibit an elongated S phase, accumulate R1 in its oxidized form and also contain significantly decreased deoxyribonucleotide levels during the S phase. Overexpressing R1 in these cells increases both the amount of the R1 reduced form and the concentrations of deoxyribonucleotides and accelerates DNA replication. These results establish thioredoxins as the major RNR reducing system in yeast and indicate that impaired RNR reduction accounts for the S phase defects of thioredoxin-deficient cells.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17349928</PMID><DateCompleted><Year>2007</Year><Month>05</Month><Day>10</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0891-5849</ISSN><JournalIssue CitedMedium="Print"><Volume>42</Volume><Issue>7</Issue><PubDate><Year>2007</Year><Month>Apr</Month><Day>01</Day></PubDate></JournalIssue><Title>Free radical biology & medicine</Title><ISOAbbreviation>Free Radic Biol Med</ISOAbbreviation></Journal><ArticleTitle>Visualization of ribonucleotide reductase catalytic oxidation establishes thioredoxins as its major reductants in yeast.</ArticleTitle><Pagination><MedlinePgn>1008-16</MedlinePgn></Pagination><Abstract><AbstractText>Thioredoxins and/or glutaredoxins assist ribonucleotide reductase, and other such enzymes that require disulfide bond reduction during their catalytic cycle. In Saccharomyces cerevisiae, the presence of either pathway is essential but which of these pathways operates in ribonucleotide reductase reduction and how this function contributes to the pathways' essential nature have not been definitively established. We have identified two in vivo redox forms of the S. cerevisiae ribonucleotide reductase R1 subunit, which correspond to catalytically reduced or oxidized enzymes. Cells lacking thioredoxins, which exhibit an elongated S phase, accumulate R1 in its oxidized form and also contain significantly decreased deoxyribonucleotide levels during the S phase. Overexpressing R1 in these cells increases both the amount of the R1 reduced form and the concentrations of deoxyribonucleotides and accelerates DNA replication. These results establish thioredoxins as the major RNR reducing system in yeast and indicate that impaired RNR reduction accounts for the S phase defects of thioredoxin-deficient cells.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Camier</LastName><ForeName>Sylvie</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>CEA, DSV, DBJC, Service de Biochimie et de Génétique Moléculaire, 91191 Gif-sur-Yvette Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ma</LastName><ForeName>Emilie</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Leroy</LastName><ForeName>Christophe</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Pruvost</LastName><ForeName>Alain</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Toledano</LastName><ForeName>Michel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Marsolier-Kergoat</LastName><ForeName>Marie-Claude</ForeName><Initials>MC</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><ArticleDate DateType="Electronic"><Year>2007</Year><Month>01</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Free Radic Biol Med</MedlineTA><NlmUniqueID>8709159</NlmUniqueID><ISSNLinking>0891-5849</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.17.4.-</RegistryNumber><NameOfSubstance UI="D012264">Ribonucleotide Reductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012264" MajorTopicYN="N">Ribonucleotide Reductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>11</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>12</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>12</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>3</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>5</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>3</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17349928</ArticleId><ArticleId IdType="pii">S0891-5849(07)00003-2</ArticleId><ArticleId IdType="doi">10.1016/j.freeradbiomed.2006.12.027</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Gif-sur-Yvette</li></settlement></list><tree><noCountry><name sortKey="Leroy, Christophe" sort="Leroy, Christophe" uniqKey="Leroy C" first="Christophe" last="Leroy">Christophe Leroy</name><name sortKey="Ma, Emilie" sort="Ma, Emilie" uniqKey="Ma E" first="Emilie" last="Ma">Emilie Ma</name><name sortKey="Marsolier Kergoat, Marie Claude" sort="Marsolier Kergoat, Marie Claude" uniqKey="Marsolier Kergoat M" first="Marie-Claude" last="Marsolier-Kergoat">Marie-Claude Marsolier-Kergoat</name><name sortKey="Pruvost, Alain" sort="Pruvost, Alain" uniqKey="Pruvost A" first="Alain" last="Pruvost">Alain Pruvost</name><name sortKey="Toledano, Michel" sort="Toledano, Michel" uniqKey="Toledano M" first="Michel" last="Toledano">Michel Toledano</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Camier, Sylvie" sort="Camier, Sylvie" uniqKey="Camier S" first="Sylvie" last="Camier">Sylvie Camier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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