Localization and function of three monothiol glutaredoxins in Schizosaccharomyces pombe.
Identifieur interne : 000E06 ( Main/Exploration ); précédent : 000E05; suivant : 000E07Localization and function of three monothiol glutaredoxins in Schizosaccharomyces pombe.
Auteurs : Woo-Hyun Chung [Corée du Sud] ; Kyoung-Dong Kim ; Jung-Hye RoeSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2005.
Descripteurs français
- KwdFr :
- Données de séquences moléculaires (MeSH), Fractions subcellulaires (métabolisme), Glutarédoxines (MeSH), Gènes fongiques (MeSH), Mitochondries (métabolisme), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Protéines de Saccharomyces cerevisiae (MeSH), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Schizosaccharomyces (génétique), Schizosaccharomyces (métabolisme), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Oxidoreductases.
- génétique : Saccharomyces cerevisiae, Schizosaccharomyces.
- métabolisme : Fractions subcellulaires, Mitochondries, Oxidoreductases, Saccharomyces cerevisiae, Schizosaccharomyces.
- Données de séquences moléculaires, Glutarédoxines, Gènes fongiques, Protéines de Saccharomyces cerevisiae, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Genes, Fungal (MeSH), Glutaredoxins (MeSH), Mitochondria (metabolism), Molecular Sequence Data (MeSH), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (MeSH), Schizosaccharomyces (genetics), Schizosaccharomyces (metabolism), Sequence Homology, Amino Acid (MeSH), Subcellular Fractions (metabolism).
- MESH :
- chemical , chemistry : Oxidoreductases.
- chemical , metabolism : Oxidoreductases.
- chemical : Glutaredoxins, Saccharomyces cerevisiae Proteins.
- genetics : Saccharomyces cerevisiae, Schizosaccharomyces.
- metabolism : Mitochondria, Saccharomyces cerevisiae, Schizosaccharomyces, Subcellular Fractions.
- Amino Acid Sequence, Genes, Fungal, Molecular Sequence Data, Sequence Homology, Amino Acid.
Abstract
The fission yeast Schizosaccharomyces pombe contains two dithiol glutaredoxins (Grx1 and Grx2) and genes for three putative monothiol glutaredoxins (grx3, 4, and 5). We investigated the expression, sub-cellular localization, and functions of the three monothiol glutaredoxins. Fluorescence microscopy revealed that Grx3 is targeted to nuclear rim and endoplasmic reticulum, Grx4 primarily to the nucleus, and Grx5 to mitochondria. Null mutation of grx3 did not significantly affect growth and resistance against various oxidants, whereas grx5 mutation caused slow growth and sensitivity toward oxidants such as hydrogen peroxide, paraquat, and diamide. The grx2grx5 double mutation, deficient in all mitochondrial glutaredoxins, caused further retardation in growth and severe sensitivity toward all the oxidants tested. The grx4 mutation was not viable, suggesting a critical role of Grx4 for the physiology of S. pombe. Overproduction of Grx3 and Grx5, but not the truncated form of Grx5 without mitochondrial target sequence, severely retarded growth as Grx2 did, supporting the idea that Grx2, 3, and 5 are targeted to organellar compartments. Our results propose a distinct role for each glutaredoxin to maintain thiol redox balance, and hence the growth and stress resistance, of the fission yeast.
DOI: 10.1016/j.bbrc.2005.02.183
PubMed: 15796926
Affiliations:
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Le document en format XML
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first="Kyoung-Dong" last="Kim">Kyoung-Dong Kim</name></author><author><name sortKey="Roe, Jung Hye" sort="Roe, Jung Hye" uniqKey="Roe J" first="Jung-Hye" last="Roe">Jung-Hye Roe</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Genes, Fungal (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Mitochondria (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidoreductases (chemistry)</term><term>Oxidoreductases (metabolism)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (MeSH)</term><term>Schizosaccharomyces (genetics)</term><term>Schizosaccharomyces (metabolism)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Subcellular Fractions (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Données de séquences moléculaires (MeSH)</term><term>Fractions subcellulaires (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Gènes fongiques (MeSH)</term><term>Mitochondries (métabolisme)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (MeSH)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Schizosaccharomyces (génétique)</term><term>Schizosaccharomyces (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Saccharomyces cerevisiae</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term><term>Saccharomyces cerevisiae</term><term>Schizosaccharomyces</term><term>Subcellular Fractions</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fractions subcellulaires</term><term>Mitochondries</term><term>Oxidoreductases</term><term>Saccharomyces cerevisiae</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Genes, Fungal</term><term>Molecular Sequence Data</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Gènes fongiques</term><term>Protéines de Saccharomyces cerevisiae</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The fission yeast Schizosaccharomyces pombe contains two dithiol glutaredoxins (Grx1 and Grx2) and genes for three putative monothiol glutaredoxins (grx3, 4, and 5). We investigated the expression, sub-cellular localization, and functions of the three monothiol glutaredoxins. Fluorescence microscopy revealed that Grx3 is targeted to nuclear rim and endoplasmic reticulum, Grx4 primarily to the nucleus, and Grx5 to mitochondria. Null mutation of grx3 did not significantly affect growth and resistance against various oxidants, whereas grx5 mutation caused slow growth and sensitivity toward oxidants such as hydrogen peroxide, paraquat, and diamide. The grx2grx5 double mutation, deficient in all mitochondrial glutaredoxins, caused further retardation in growth and severe sensitivity toward all the oxidants tested. The grx4 mutation was not viable, suggesting a critical role of Grx4 for the physiology of S. pombe. Overproduction of Grx3 and Grx5, but not the truncated form of Grx5 without mitochondrial target sequence, severely retarded growth as Grx2 did, supporting the idea that Grx2, 3, and 5 are targeted to organellar compartments. Our results propose a distinct role for each glutaredoxin to maintain thiol redox balance, and hence the growth and stress resistance, of the fission yeast.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15796926</PMID><DateCompleted><Year>2005</Year><Month>06</Month><Day>07</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>330</Volume><Issue>2</Issue><PubDate><Year>2005</Year><Month>May</Month><Day>06</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Localization and function of three monothiol glutaredoxins in Schizosaccharomyces pombe.</ArticleTitle><Pagination><MedlinePgn>604-10</MedlinePgn></Pagination><Abstract><AbstractText>The fission yeast Schizosaccharomyces pombe contains two dithiol glutaredoxins (Grx1 and Grx2) and genes for three putative monothiol glutaredoxins (grx3, 4, and 5). We investigated the expression, sub-cellular localization, and functions of the three monothiol glutaredoxins. Fluorescence microscopy revealed that Grx3 is targeted to nuclear rim and endoplasmic reticulum, Grx4 primarily to the nucleus, and Grx5 to mitochondria. Null mutation of grx3 did not significantly affect growth and resistance against various oxidants, whereas grx5 mutation caused slow growth and sensitivity toward oxidants such as hydrogen peroxide, paraquat, and diamide. The grx2grx5 double mutation, deficient in all mitochondrial glutaredoxins, caused further retardation in growth and severe sensitivity toward all the oxidants tested. The grx4 mutation was not viable, suggesting a critical role of Grx4 for the physiology of S. pombe. Overproduction of Grx3 and Grx5, but not the truncated form of Grx5 without mitochondrial target sequence, severely retarded growth as Grx2 did, supporting the idea that Grx2, 3, and 5 are targeted to organellar compartments. Our results propose a distinct role for each glutaredoxin to maintain thiol redox balance, and hence the growth and stress resistance, of the fission yeast.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chung</LastName><ForeName>Woo-Hyun</ForeName><Initials>WH</Initials><AffiliationInfo><Affiliation>Laboratory of Molecular Microbiology, School of Biological Sciences, Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Kyoung-Dong</ForeName><Initials>KD</Initials></Author><Author ValidYN="Y"><LastName>Roe</LastName><ForeName>Jung-Hye</ForeName><Initials>JH</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>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516012">Grx4 protein, S cerevisiae</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005800" MajorTopicYN="N">Genes, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013347" MajorTopicYN="N">Subcellular Fractions</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2005</Year><Month>02</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>3</Month><Day>31</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>6</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>3</Month><Day>31</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15796926</ArticleId><ArticleId IdType="pii">S0006-291X(05)00431-6</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2005.02.183</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country><region><li>Région capitale de Séoul</li></region><settlement><li>Séoul</li></settlement><orgName><li>Université nationale de Séoul</li></orgName></list><tree><noCountry><name sortKey="Kim, Kyoung Dong" sort="Kim, Kyoung Dong" uniqKey="Kim K" first="Kyoung-Dong" last="Kim">Kyoung-Dong Kim</name><name sortKey="Roe, Jung Hye" sort="Roe, Jung Hye" uniqKey="Roe J" first="Jung-Hye" last="Roe">Jung-Hye Roe</name></noCountry><country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Chung, Woo Hyun" sort="Chung, Woo Hyun" uniqKey="Chung W" first="Woo-Hyun" last="Chung">Woo-Hyun Chung</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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