Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils.
Identifieur interne : 000B02 ( Main/Exploration ); précédent : 000B01; suivant : 000B03Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils.
Auteurs : Zai-Rong Zhang [République populaire de Chine] ; Sarah PerrettSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2009.
Descripteurs français
- KwdFr :
- Amyloïde (effets des médicaments et des substances chimiques), Amyloïde (métabolisme), Biocatalyse (effets des médicaments et des substances chimiques), Chlorure de cadmium (pharmacologie), Cinétique (MeSH), Facteurs temps (MeSH), Glutarédoxines (métabolisme), Glutathion (métabolisme), Glutathione peroxidase (MeSH), Insuline (métabolisme), Multimérisation de protéines (effets des médicaments et des substances chimiques), Mutation (génétique), Oxidoreductases (MeSH), Oxydoréduction (effets des médicaments et des substances chimiques), Peroxyde d'hydrogène (pharmacologie), Prions (composition chimique), Prions (métabolisme), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (métabolisme), Réducteurs (pharmacologie), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (enzymologie), Sites de fixation (MeSH), Solubilité (effets des médicaments et des substances chimiques), Structure tertiaire des protéines (MeSH).
- MESH :
- composition chimique : Prions, Protéines de Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Amyloïde, Biocatalyse, Multimérisation de protéines, Oxydoréduction, Saccharomyces cerevisiae, Solubilité.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Mutation.
- métabolisme : Amyloïde, Glutarédoxines, Glutathion, Insuline, Prions, Protéines de Saccharomyces cerevisiae.
- pharmacologie : Chlorure de cadmium, Peroxyde d'hydrogène, Réducteurs.
- Cinétique, Facteurs temps, Glutathione peroxidase, Oxidoreductases, Sites de fixation, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Amyloid (drug effects), Amyloid (metabolism), Binding Sites (MeSH), Biocatalysis (drug effects), Cadmium Chloride (pharmacology), Glutaredoxins (metabolism), Glutathione (metabolism), Glutathione Peroxidase (MeSH), Hydrogen Peroxide (pharmacology), Insulin (metabolism), Kinetics (MeSH), Mutation (genetics), Oxidation-Reduction (drug effects), Oxidoreductases (MeSH), Prions (chemistry), Prions (metabolism), Protein Multimerization (drug effects), Protein Structure, Tertiary (MeSH), Reducing Agents (pharmacology), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism), Solubility (drug effects), Time Factors (MeSH).
- MESH :
- chemical , chemistry : Prions, Saccharomyces cerevisiae Proteins.
- chemical , drug effects : Amyloid.
- chemical , metabolism : Amyloid, Glutaredoxins, Glutathione, Insulin, Prions, Saccharomyces cerevisiae Proteins.
- drug effects : Biocatalysis, Oxidation-Reduction, Protein Multimerization, Saccharomyces cerevisiae, Solubility.
- enzymology : Saccharomyces cerevisiae.
- genetics : Mutation.
- chemical , pharmacology : Cadmium Chloride, Hydrogen Peroxide, Reducing Agents.
- Binding Sites, Glutathione Peroxidase, Kinetics, Oxidoreductases, Protein Structure, Tertiary, Time Factors.
Abstract
Ure2 is the protein determinant of the Saccharomyces cerevisiae prion [URE3]. Ure2 has structural similarity to glutathione transferases, protects cells against heavy metal and oxidant toxicity in vivo, and shows glutathione-dependent peroxidase activity in vitro. Here we report that Ure2 (which has no cysteine residues) also shows thiol-disulfide oxidoreductase activity similar to that of glutaredoxin enzymes. This demonstrates that disulfide reductase activity can be independent of the classical glutaredoxin CXXC/CXXS motif or indeed an intrinsic catalytic cysteine residue. The kinetics of the glutaredoxin activity of Ure2 showed positive cooperativity for the substrate glutathione in both the soluble native state and in amyloid-like fibrils, indicating native-like dimeric structure within Ure2 fibrils. Characterization of the glutaredoxin activity of Ure2 sheds light on its ability to protect yeast from heavy metal ion and oxidant toxicity and suggests a role in reversible protein glutathionylation signal transduction. Observation of allosteric enzyme behavior within amyloid-like Ure2 fibrils not only provides insight into the molecular structure of the fibrils but also has implications for the mechanism of [URE3] prion formation.
DOI: 10.1074/jbc.M901189200
PubMed: 19321443
PubMed Central: PMC2682854
Affiliations:
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Le document en format XML
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protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ure2 is the protein determinant of the Saccharomyces cerevisiae prion [URE3]. Ure2 has structural similarity to glutathione transferases, protects cells against heavy metal and oxidant toxicity in vivo, and shows glutathione-dependent peroxidase activity in vitro. Here we report that Ure2 (which has no cysteine residues) also shows thiol-disulfide oxidoreductase activity similar to that of glutaredoxin enzymes. This demonstrates that disulfide reductase activity can be independent of the classical glutaredoxin CXXC/CXXS motif or indeed an intrinsic catalytic cysteine residue. The kinetics of the glutaredoxin activity of Ure2 showed positive cooperativity for the substrate glutathione in both the soluble native state and in amyloid-like fibrils, indicating native-like dimeric structure within Ure2 fibrils. Characterization of the glutaredoxin activity of Ure2 sheds light on its ability to protect yeast from heavy metal ion and oxidant toxicity and suggests a role in reversible protein glutathionylation signal transduction. Observation of allosteric enzyme behavior within amyloid-like Ure2 fibrils not only provides insight into the molecular structure of the fibrils but also has implications for the mechanism of [URE3] prion formation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19321443</PMID><DateCompleted><Year>2009</Year><Month>07</Month><Day>07</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>284</Volume><Issue>21</Issue><PubDate><Year>2009</Year><Month>May</Month><Day>22</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils.</ArticleTitle><Pagination><MedlinePgn>14058-67</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M901189200</ELocationID><Abstract><AbstractText>Ure2 is the protein determinant of the Saccharomyces cerevisiae prion [URE3]. Ure2 has structural similarity to glutathione transferases, protects cells against heavy metal and oxidant toxicity in vivo, and shows glutathione-dependent peroxidase activity in vitro. Here we report that Ure2 (which has no cysteine residues) also shows thiol-disulfide oxidoreductase activity similar to that of glutaredoxin enzymes. This demonstrates that disulfide reductase activity can be independent of the classical glutaredoxin CXXC/CXXS motif or indeed an intrinsic catalytic cysteine residue. The kinetics of the glutaredoxin activity of Ure2 showed positive cooperativity for the substrate glutathione in both the soluble native state and in amyloid-like fibrils, indicating native-like dimeric structure within Ure2 fibrils. Characterization of the glutaredoxin activity of Ure2 sheds light on its ability to protect yeast from heavy metal ion and oxidant toxicity and suggests a role in reversible protein glutathionylation signal transduction. Observation of allosteric enzyme behavior within amyloid-like Ure2 fibrils not only provides insight into the molecular structure of the fibrils but also has implications for the mechanism of [URE3] prion formation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Zai-Rong</ForeName><Initials>ZR</Initials><AffiliationInfo><Affiliation>National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Perrett</LastName><ForeName>Sarah</ForeName><Initials>S</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>2009</Year><Month>03</Month><Day>25</Day></ArticleDate></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="D000682">Amyloid</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007328">Insulin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011328">Prions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019163">Reducing Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae 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Chloride</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000682" MajorTopicYN="N">Amyloid</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055162" MajorTopicYN="N">Biocatalysis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019256" MajorTopicYN="N">Cadmium Chloride</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" 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IdType="pubmed">12933788</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2004 Feb;6(1):63-74</Citation><ArticleIdList><ArticleId IdType="pubmed">14713336</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 May 25;101(21):7885-90</Citation><ArticleIdList><ArticleId IdType="pubmed">15143215</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1976 Jul;73(7):2275-9</Citation><ArticleIdList><ArticleId IdType="pubmed">7783</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2000 Aug 11;275(32):24798-806</Citation><ArticleIdList><ArticleId IdType="pubmed">10783391</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2000 Aug 25;275(34):26556-65</Citation><ArticleIdList><ArticleId IdType="pubmed">10854441</ArticleId></ArticleIdList></Reference><Reference><Citation>J Cell Biol. 2001 Jun 11;153(6):1327-36</Citation><ArticleIdList><ArticleId IdType="pubmed">11402074</ArticleId></ArticleIdList></Reference><Reference><Citation>Structure. 2001 Jan 10;9(1):39-46</Citation><ArticleIdList><ArticleId IdType="pubmed">11342133</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 2001 Nov 15;360(Pt 1):1-16</Citation><ArticleIdList><ArticleId IdType="pubmed">11695986</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2001 Nov 13;40(45):13564-73</Citation><ArticleIdList><ArticleId IdType="pubmed">11695904</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5253-60</Citation><ArticleIdList><ArticleId IdType="pubmed">11959975</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2002 May 10;277(19):16712-7</Citation><ArticleIdList><ArticleId IdType="pubmed">11875065</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2002 May 24;277(21):18777-84</Citation><ArticleIdList><ArticleId IdType="pubmed">11889135</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2002 Jun 17;21(12):2903-11</Citation><ArticleIdList><ArticleId IdType="pubmed">12065404</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 Apr 11;278(15):12826-33</Citation><ArticleIdList><ArticleId IdType="pubmed">12562760</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 Jun 20;278(25):22325-30</Citation><ArticleIdList><ArticleId IdType="pubmed">12682041</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1979 Oct 10;254(19):9627-32</Citation><ArticleIdList><ArticleId IdType="pubmed">385588</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1989 Nov 1;182(2):319-26</Citation><ArticleIdList><ArticleId IdType="pubmed">2610349</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1990 Sep 15;265(26):15361-4</Citation><ArticleIdList><ArticleId IdType="pubmed">2394726</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1994 Jan;216(1):15-26</Citation><ArticleIdList><ArticleId IdType="pubmed">8135345</ArticleId></ArticleIdList></Reference><Reference><Citation>Structure. 1995 Mar 15;3(3):245-50</Citation><ArticleIdList><ArticleId IdType="pubmed">7788290</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1995;252:30-8</Citation><ArticleIdList><ArticleId IdType="pubmed">7476366</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1995;252:283-92</Citation><ArticleIdList><ArticleId IdType="pubmed">7476363</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1999 Jul 2;290(1):331-45</Citation><ArticleIdList><ArticleId IdType="pubmed">10388576</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1959 May;82(1):70-7</Citation><ArticleIdList><ArticleId IdType="pubmed">13650640</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 Nov 26;279(48):50025-30</Citation><ArticleIdList><ArticleId IdType="pubmed">15371425</ArticleId></ArticleIdList></Reference><Reference><Citation>Yeast. 2005 Apr 15;22(5):343-58</Citation><ArticleIdList><ArticleId IdType="pubmed">15806612</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2005 Nov 4;280(44):37149-58</Citation><ArticleIdList><ArticleId IdType="pubmed">16131495</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 2005;401:78-99</Citation><ArticleIdList><ArticleId IdType="pubmed">16399380</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 2006 Sep 1;398(2):187-96</Citation><ArticleIdList><ArticleId IdType="pubmed">16709151</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Nov 3;281(44):33107-14</Citation><ArticleIdList><ArticleId IdType="pubmed">16956877</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Mol Life Sci. 2007 Jun;64(12):1518-30</Citation><ArticleIdList><ArticleId IdType="pubmed">17415523</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Pharmacol. 2007 Aug;7(4):381-91</Citation><ArticleIdList><ArticleId IdType="pubmed">17662654</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2008 Feb 5;47(5):1452-63</Citation><ArticleIdList><ArticleId IdType="pubmed">18171082</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 Apr 4;283(14):8868-76</Citation><ArticleIdList><ArticleId IdType="pubmed">18216016</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2008 Jun;19(6):2673-80</Citation><ArticleIdList><ArticleId IdType="pubmed">18400945</ArticleId></ArticleIdList></Reference><Reference><Citation>Proteins. 2008 Aug 15;72(3):1077-83</Citation><ArticleIdList><ArticleId IdType="pubmed">18473363</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2008 Nov;1780(11):1304-17</Citation><ArticleIdList><ArticleId IdType="pubmed">18621099</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2008 Dec 19;384(3):641-51</Citation><ArticleIdList><ArticleId IdType="pubmed">18845158</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 2009 Jan 1;417(1):55-64</Citation><ArticleIdList><ArticleId IdType="pubmed">18778244</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2009 Jan 23;385(3):889-901</Citation><ArticleIdList><ArticleId IdType="pubmed">18992757</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1996 Nov 1;335(1):61-72</Citation><ArticleIdList><ArticleId IdType="pubmed">8914835</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 Oct 31;278(44):43717-27</Citation><ArticleIdList><ArticleId IdType="pubmed">12917441</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><noCountry><name sortKey="Perrett, Sarah" sort="Perrett, Sarah" uniqKey="Perrett S" first="Sarah" last="Perrett">Sarah Perrett</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Zhang, Zai Rong" sort="Zhang, Zai Rong" uniqKey="Zhang Z" first="Zai-Rong" last="Zhang">Zai-Rong Zhang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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