Predictive reconstruction of the mitochondrial iron-sulfur cluster assembly metabolism. II. Role of glutaredoxin Grx5.
Identifieur interne : 000E62 ( Main/Exploration ); précédent : 000E61; suivant : 000E63Predictive reconstruction of the mitochondrial iron-sulfur cluster assembly metabolism. II. Role of glutaredoxin Grx5.
Auteurs : Rui Alves [Espagne] ; Enrique Herrero ; Albert SorribasSource :
- Proteins [ 1097-0134 ] ; 2004.
Descripteurs français
- KwdFr :
- Biologie informatique (MeSH), Carbon-sulfur lyases (composition chimique), Carbon-sulfur lyases (génétique), Carbon-sulfur lyases (métabolisme), Cinétique (MeSH), Conformation des protéines (MeSH), Cystéine (composition chimique), Cystéine (métabolisme), Disulfures (composition chimique), Disulfures (métabolisme), Ferrosulfoprotéines (biosynthèse), Ferrosulfoprotéines (composition chimique), Glutarédoxines (MeSH), Liaison aux protéines (MeSH), Mathématiques (MeSH), Mitochondries (enzymologie), Mitochondries (métabolisme), Modèles biologiques (MeSH), Modèles moléculaires (MeSH), Mutation (génétique), Oxidoreductases (composition chimique), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines mitochondriales (biosynthèse), Protéines mitochondriales (composition chimique), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sulfurtransferases (MeSH).
- MESH :
- biosynthèse : Ferrosulfoprotéines, Protéines mitochondriales.
- composition chimique : Carbon-sulfur lyases, Cystéine, Disulfures, Ferrosulfoprotéines, Oxidoreductases, Protéines de Saccharomyces cerevisiae, Protéines mitochondriales.
- cytologie : Saccharomyces cerevisiae.
- enzymologie : Mitochondries.
- génétique : Carbon-sulfur lyases, Mutation, Oxidoreductases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Carbon-sulfur lyases, Cystéine, Disulfures, Mitochondries, Oxidoreductases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- Biologie informatique, Cinétique, Conformation des protéines, Glutarédoxines, Liaison aux protéines, Mathématiques, Modèles biologiques, Modèles moléculaires, Oxydoréduction, Sulfurtransferases.
English descriptors
- KwdEn :
- Carbon-Sulfur Lyases (chemistry), Carbon-Sulfur Lyases (genetics), Carbon-Sulfur Lyases (metabolism), Computational Biology (MeSH), Cysteine (chemistry), Cysteine (metabolism), Disulfides (chemistry), Disulfides (metabolism), Glutaredoxins (MeSH), Iron-Sulfur Proteins (biosynthesis), Iron-Sulfur Proteins (chemistry), Kinetics (MeSH), Mathematics (MeSH), Mitochondria (enzymology), Mitochondria (metabolism), Mitochondrial Proteins (biosynthesis), Mitochondrial Proteins (chemistry), Models, Biological (MeSH), Models, Molecular (MeSH), Mutation (genetics), Oxidation-Reduction (MeSH), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Protein Binding (MeSH), Protein Conformation (MeSH), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sulfurtransferases (MeSH).
- MESH :
- chemical , biosynthesis : Iron-Sulfur Proteins, Mitochondrial Proteins.
- chemical , chemistry : Carbon-Sulfur Lyases, Cysteine, Disulfides, Iron-Sulfur Proteins, Mitochondrial Proteins, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Carbon-Sulfur Lyases, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Carbon-Sulfur Lyases, Cysteine, Disulfides, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- cytology : Saccharomyces cerevisiae.
- enzymology : Mitochondria.
- genetics : Mutation, Saccharomyces cerevisiae.
- metabolism : Mitochondria, Saccharomyces cerevisiae.
- Computational Biology, Glutaredoxins, Kinetics, Mathematics, Models, Biological, Models, Molecular, Oxidation-Reduction, Protein Binding, Protein Conformation, Sulfurtransferases.
Abstract
Grx5 is a Saccharomyces cerevisiae glutaredoxin involved in iron-sulfur cluster (FeSC) biogenesis. Previous work suggests that Grx5 is involved in regulating protein cysteine glutathionylation, prompting several questions about the systemic role of Grx5. First, is the regulation of mixed protein-glutathione disulfide bridges in FeSC biosynthetic proteins by Grx5 sufficient to account for the observed phenotypes of the Deltagrx5 mutants? If so, does Grx5 regulate the oxidation state of mixed protein-glutathione disulfide bridges in FeSC biogenesis in general? Alternatively, can the Deltagrx5 mutant phenotypes be explained if Grx5 acts on just one or a few of the FeSC biogenesis proteins?In the first part of this article, we address these questions by building and analyzing a mathematical model of FeSC biosynthesis. We show that, independent of the tested parameter values, the dynamic behavior observed in cells depleted of Grx5 can only be qualitatively reproduced if Grx5 acts by regulating the initial assembly of FeSC in scaffold proteins. This can be achieved by acting on the cysteine desulfurase (Nfs1) activity and/or on scaffold functionality. In the second part of this article, we use structural bioinformatics methods to evaluate the possibility of interaction between Grx5 and proteins involved in FeSC biogenesis. Based on such methods, our results indicate that the proteins with which Grx5 is more likely to interact are consistent with the kinetic modeling results.Thus, our theoretical studies, combined with known Grx5 biochemistry, suggest that Grx5 acts on FeSC biosynthesis by regulating the redox state of important cysteine residues in Nfs1 and/or in the scaffold proteins where FeSC initially assemble.
DOI: 10.1002/prot.20228
PubMed: 15382238
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Conformation</term><term>Sulfurtransferases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biologie informatique</term><term>Cinétique</term><term>Conformation des protéines</term><term>Glutarédoxines</term><term>Liaison aux protéines</term><term>Mathématiques</term><term>Modèles biologiques</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Sulfurtransferases</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Grx5 is a Saccharomyces cerevisiae glutaredoxin involved in iron-sulfur cluster (FeSC) biogenesis. Previous work suggests that Grx5 is involved in regulating protein cysteine glutathionylation, prompting several questions about the systemic role of Grx5. First, is the regulation of mixed protein-glutathione disulfide bridges in FeSC biosynthetic proteins by Grx5 sufficient to account for the observed phenotypes of the Deltagrx5 mutants? If so, does Grx5 regulate the oxidation state of mixed protein-glutathione disulfide bridges in FeSC biogenesis in general? Alternatively, can the Deltagrx5 mutant phenotypes be explained if Grx5 acts on just one or a few of the FeSC biogenesis proteins?In the first part of this article, we address these questions by building and analyzing a mathematical model of FeSC biosynthesis. We show that, independent of the tested parameter values, the dynamic behavior observed in cells depleted of Grx5 can only be qualitatively reproduced if Grx5 acts by regulating the initial assembly of FeSC in scaffold proteins. This can be achieved by acting on the cysteine desulfurase (Nfs1) activity and/or on scaffold functionality. In the second part of this article, we use structural bioinformatics methods to evaluate the possibility of interaction between Grx5 and proteins involved in FeSC biogenesis. Based on such methods, our results indicate that the proteins with which Grx5 is more likely to interact are consistent with the kinetic modeling results.Thus, our theoretical studies, combined with known Grx5 biochemistry, suggest that Grx5 acts on FeSC biosynthesis by regulating the redox state of important cysteine residues in Nfs1 and/or in the scaffold proteins where FeSC initially assemble.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15382238</PMID><DateCompleted><Year>2005</Year><Month>11</Month><Day>01</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1097-0134</ISSN><JournalIssue CitedMedium="Internet"><Volume>57</Volume><Issue>3</Issue><PubDate><Year>2004</Year><Month>Nov</Month><Day>15</Day></PubDate></JournalIssue><Title>Proteins</Title><ISOAbbreviation>Proteins</ISOAbbreviation></Journal><ArticleTitle>Predictive reconstruction of the mitochondrial iron-sulfur cluster assembly metabolism. II. Role of glutaredoxin Grx5.</ArticleTitle><Pagination><MedlinePgn>481-92</MedlinePgn></Pagination><Abstract><AbstractText>Grx5 is a Saccharomyces cerevisiae glutaredoxin involved in iron-sulfur cluster (FeSC) biogenesis. Previous work suggests that Grx5 is involved in regulating protein cysteine glutathionylation, prompting several questions about the systemic role of Grx5. First, is the regulation of mixed protein-glutathione disulfide bridges in FeSC biosynthetic proteins by Grx5 sufficient to account for the observed phenotypes of the Deltagrx5 mutants? If so, does Grx5 regulate the oxidation state of mixed protein-glutathione disulfide bridges in FeSC biogenesis in general? Alternatively, can the Deltagrx5 mutant phenotypes be explained if Grx5 acts on just one or a few of the FeSC biogenesis proteins?In the first part of this article, we address these questions by building and analyzing a mathematical model of FeSC biosynthesis. We show that, independent of the tested parameter values, the dynamic behavior observed in cells depleted of Grx5 can only be qualitatively reproduced if Grx5 acts by regulating the initial assembly of FeSC in scaffold proteins. This can be achieved by acting on the cysteine desulfurase (Nfs1) activity and/or on scaffold functionality. In the second part of this article, we use structural bioinformatics methods to evaluate the possibility of interaction between Grx5 and proteins involved in FeSC biogenesis. Based on such methods, our results indicate that the proteins with which Grx5 is more likely to interact are consistent with the kinetic modeling results.Thus, our theoretical studies, combined with known Grx5 biochemistry, suggest that Grx5 acts on FeSC biosynthesis by regulating the redox state of important cysteine residues in Nfs1 and/or in the scaffold proteins where FeSC initially assemble.</AbstractText><CopyrightInformation>(c) 2004 Wiley-Liss, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Alves</LastName><ForeName>Rui</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Departament de Ciencies Mediques Basiques, Universidad de Lleida, Lleida, Spain. ralves@cmb.udl.es </Affiliation> </AffiliationInfo></Author><Author ValidYN="Y"><LastName>Herrero</LastName><ForeName>Enrique</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Sorribas</LastName><ForeName>Albert</ForeName><Initials>A</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>Proteins</MedlineTA><NlmUniqueID>8700181</NlmUniqueID><ISSNLinking>0887-3585</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024101">Mitochondrial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.8.1.-</RegistryNumber><NameOfSubstance UI="D013466">Sulfurtransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.8.1.7</RegistryNumber><NameOfSubstance UI="C115912">NFS1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.4.-</RegistryNumber><NameOfSubstance UI="D013437">Carbon-Sulfur Lyases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.4.1.-</RegistryNumber><NameOfSubstance UI="C080546">cysteine desulfurase</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D013437" MajorTopicYN="N">Carbon-Sulfur Lyases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019295" MajorTopicYN="N">Computational Biology</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008433" MajorTopicYN="N">Mathematics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D024101" MajorTopicYN="N">Mitochondrial Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013466" MajorTopicYN="N">Sulfurtransferases</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>9</Month><Day>24</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>11</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>9</Month><Day>24</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15382238</ArticleId><ArticleId IdType="doi">10.1002/prot.20228</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country></list><tree><noCountry><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" uniqKey="Herrero E" first="Enrique" last="Herrero">Enrique Herrero</name><name sortKey="Sorribas, Albert" sort="Sorribas, Albert" uniqKey="Sorribas A" first="Albert" last="Sorribas">Albert Sorribas</name></noCountry><country name="Espagne"><noRegion><name sortKey="Alves, Rui" sort="Alves, Rui" uniqKey="Alves R" first="Rui" last="Alves">Rui Alves</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |