Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway.
Identifieur interne : 000B69 ( Main/Exploration ); précédent : 000B68; suivant : 000B70Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway.
Auteurs : Alicia Izquierdo [Espagne] ; Celia Casas ; Ulrich Mühlenhoff ; Christopher Horst Lillig ; Enrique HerreroSource :
- Eukaryotic cell [ 1535-9786 ] ; 2008.
Descripteurs français
- KwdFr :
- Antienzymes (pharmacologie), Appareil de Golgi (métabolisme), Appareil de Golgi (ultrastructure), Facteurs de transcription (métabolisme), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glycosylation (effets des médicaments et des substances chimiques), Oxidoreductases acting on sulfur group donors (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de liaison à l'ADN (métabolisme), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Régulation de l'expression des gènes fongiques (physiologie), Réticulum endoplasmique (métabolisme), Réticulum endoplasmique (ultrastructure), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Transduction du signal (génétique), Vésicules de sécrétion (génétique), Vésicules de sécrétion (métabolisme), Vésicules de sécrétion (ultrastructure).
- MESH :
- effets des médicaments et des substances chimiques : Glycosylation, Régulation de l'expression des gènes fongiques.
- génétique : Glutarédoxines, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Transduction du signal, Vésicules de sécrétion.
- métabolisme : Appareil de Golgi, Facteurs de transcription, Glutarédoxines, Oxidoreductases acting on sulfur group donors, Protéines de Saccharomyces cerevisiae, Protéines de liaison à l'ADN, Réticulum endoplasmique, Saccharomyces cerevisiae, Vésicules de sécrétion.
- pharmacologie : Antienzymes.
- physiologie : Régulation de l'expression des gènes fongiques.
- ultrastructure : Appareil de Golgi, Réticulum endoplasmique, Vésicules de sécrétion.
English descriptors
- KwdEn :
- DNA-Binding Proteins (metabolism), Endoplasmic Reticulum (metabolism), Endoplasmic Reticulum (ultrastructure), Enzyme Inhibitors (pharmacology), Gene Expression Regulation, Fungal (drug effects), Gene Expression Regulation, Fungal (physiology), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glycosylation (drug effects), Golgi Apparatus (metabolism), Golgi Apparatus (ultrastructure), Oxidoreductases Acting on Sulfur Group Donors (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Secretory Vesicles (genetics), Secretory Vesicles (metabolism), Secretory Vesicles (ultrastructure), Signal Transduction (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , genetics : Glutaredoxins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : DNA-Binding Proteins, Glutaredoxins, Oxidoreductases Acting on Sulfur Group Donors, Saccharomyces cerevisiae Proteins, Transcription Factors.
- drug effects : Gene Expression Regulation, Fungal, Glycosylation.
- genetics : Saccharomyces cerevisiae, Secretory Vesicles, Signal Transduction.
- metabolism : Endoplasmic Reticulum, Golgi Apparatus, Saccharomyces cerevisiae, Secretory Vesicles.
- chemical , pharmacology : Enzyme Inhibitors.
- physiology : Gene Expression Regulation, Fungal.
- ultrastructure : Endoplasmic Reticulum, Golgi Apparatus, Secretory Vesicles.
Abstract
Saccharomyces cerevisiae Grx6 and Grx7 are two monothiol glutaredoxins whose active-site sequences (CSYS and CPYS, respectively) are reminiscent of the CPYC active-site sequence of classical dithiol glutaredoxins. Both proteins contain an N-terminal transmembrane domain which is responsible for their association to membranes of the early secretory pathway vesicles, facing the luminal side. Thus, Grx6 localizes at the endoplasmic reticulum and Golgi compartments, while Grx7 is mostly at the Golgi. Expression of GRX6 is modestly upregulated by several stresses (calcium, sodium, and peroxides) in a manner dependent on the Crz1-calcineurin pathway. Some of these stresses also upregulate GRX7 expression under the control of the Msn2/4 transcription factor. The N glycosylation inhibitor tunicamycin induces the expression of both genes along with protein accumulation. Mutants lacking both glutaredoxins display reduced sensitivity to tunicamycin, although the drug is still able to manifest its inhibitory effect on a reporter glycoprotein. Grx6 and Grx7 have measurable oxidoreductase activity in vivo, which is increased in the presence of tunicamycin. Both glutaredoxins could be responsible for the regulation of the sulfhydryl oxidative state at the oxidant conditions of the early secretory pathway vesicles. However, the differences in location and expression responses against stresses suggest that their functions are not totally overlapping.
DOI: 10.1128/EC.00133-08
PubMed: 18503006
PubMed Central: PMC2519769
Affiliations:
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Le document en format XML
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xml:lang="fr"><term>Antienzymes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Enzyme Inhibitors</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Régulation de l'expression des gènes fongiques</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Gene Expression Regulation, Fungal</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Endoplasmic Reticulum</term><term>Golgi Apparatus</term><term>Secretory Vesicles</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Appareil de Golgi</term><term>Réticulum endoplasmique</term><term>Vésicules de sécrétion</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Saccharomyces cerevisiae Grx6 and Grx7 are two monothiol glutaredoxins whose active-site sequences (CSYS and CPYS, respectively) are reminiscent of the CPYC active-site sequence of classical dithiol glutaredoxins. Both proteins contain an N-terminal transmembrane domain which is responsible for their association to membranes of the early secretory pathway vesicles, facing the luminal side. Thus, Grx6 localizes at the endoplasmic reticulum and Golgi compartments, while Grx7 is mostly at the Golgi. Expression of GRX6 is modestly upregulated by several stresses (calcium, sodium, and peroxides) in a manner dependent on the Crz1-calcineurin pathway. Some of these stresses also upregulate GRX7 expression under the control of the Msn2/4 transcription factor. The N glycosylation inhibitor tunicamycin induces the expression of both genes along with protein accumulation. Mutants lacking both glutaredoxins display reduced sensitivity to tunicamycin, although the drug is still able to manifest its inhibitory effect on a reporter glycoprotein. Grx6 and Grx7 have measurable oxidoreductase activity in vivo, which is increased in the presence of tunicamycin. Both glutaredoxins could be responsible for the regulation of the sulfhydryl oxidative state at the oxidant conditions of the early secretory pathway vesicles. However, the differences in location and expression responses against stresses suggest that their functions are not totally overlapping.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18503006</PMID><DateCompleted><Year>2008</Year><Month>10</Month><Day>24</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1535-9786</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>8</Issue><PubDate><Year>2008</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Eukaryotic cell</Title><ISOAbbreviation>Eukaryot Cell</ISOAbbreviation></Journal><ArticleTitle>Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway.</ArticleTitle><Pagination><MedlinePgn>1415-26</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/EC.00133-08</ELocationID><Abstract><AbstractText>Saccharomyces cerevisiae Grx6 and Grx7 are two monothiol glutaredoxins whose active-site sequences (CSYS and CPYS, respectively) are reminiscent of the CPYC active-site sequence of classical dithiol glutaredoxins. Both proteins contain an N-terminal transmembrane domain which is responsible for their association to membranes of the early secretory pathway vesicles, facing the luminal side. Thus, Grx6 localizes at the endoplasmic reticulum and Golgi compartments, while Grx7 is mostly at the Golgi. Expression of GRX6 is modestly upregulated by several stresses (calcium, sodium, and peroxides) in a manner dependent on the Crz1-calcineurin pathway. Some of these stresses also upregulate GRX7 expression under the control of the Msn2/4 transcription factor. The N glycosylation inhibitor tunicamycin induces the expression of both genes along with protein accumulation. Mutants lacking both glutaredoxins display reduced sensitivity to tunicamycin, although the drug is still able to manifest its inhibitory effect on a reporter glycoprotein. Grx6 and Grx7 have measurable oxidoreductase activity in vivo, which is increased in the presence of tunicamycin. Both glutaredoxins could be responsible for the regulation of the sulfhydryl oxidative state at the oxidant conditions of the early secretory pathway vesicles. However, the differences in location and expression responses against stresses suggest that their functions are not totally overlapping.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Izquierdo</LastName><ForeName>Alicia</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, Montserrat Roig 2, 25008 Lleida, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Casas</LastName><ForeName>Celia</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Mühlenhoff</LastName><ForeName>Ulrich</ForeName><Initials>U</Initials></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Herrero</LastName><ForeName>Enrique</ForeName><Initials>E</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>2008</Year><Month>05</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Eukaryot Cell</MedlineTA><NlmUniqueID>101130731</NlmUniqueID><ISSNLinking>1535-9786</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C532450">GRX7 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C527470">Grx6 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C081935">MSN2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.-</RegistryNumber><NameOfSubstance UI="D050862">Oxidoreductases Acting on Sulfur Group Donors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.-</RegistryNumber><NameOfSubstance UI="C080499">sulfide oxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004721" MajorTopicYN="N">Endoplasmic Reticulum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006056" MajorTopicYN="N">Golgi Apparatus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050862" MajorTopicYN="N">Oxidoreductases Acting on Sulfur Group Donors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D022142" MajorTopicYN="N">Secretory Vesicles</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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