Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast.
Identifieur interne : 000A15 ( Main/Exploration ); précédent : 000A14; suivant : 000A16Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast.
Auteurs : Kyoung-Dong Kim [Corée du Sud] ; Woo-Hyun Chung ; Hyo-Jin Kim ; Kyung-Chang Lee ; Jung-Hye RoeSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2010.
Descripteurs français
- KwdFr :
- ADN mitochondrial (métabolisme), Cystéine (métabolisme), Ferrosulfoprotéines (génétique), Ferrosulfoprotéines (métabolisme), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glycérol (métabolisme), Mitochondries (métabolisme), Protéines de Schizosaccharomyces pombe (génétique), Protéines de Schizosaccharomyces pombe (métabolisme), Schizosaccharomyces (croissance et développement), Schizosaccharomyces (génétique), Schizosaccharomyces (métabolisme).
- MESH :
- croissance et développement : Schizosaccharomyces.
- génétique : Ferrosulfoprotéines, Glutarédoxines, Protéines de Schizosaccharomyces pombe, Schizosaccharomyces.
- métabolisme : ADN mitochondrial, Cystéine, Ferrosulfoprotéines, Glutarédoxines, Glycérol, Mitochondries, Protéines de Schizosaccharomyces pombe, Schizosaccharomyces.
English descriptors
- KwdEn :
- Cysteine (metabolism), DNA, Mitochondrial (metabolism), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glycerol (metabolism), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Mitochondria (metabolism), Schizosaccharomyces (genetics), Schizosaccharomyces (growth & development), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (metabolism).
- MESH :
- chemical , genetics : Glutaredoxins, Iron-Sulfur Proteins, Schizosaccharomyces pombe Proteins.
- chemical , metabolism : Cysteine, DNA, Mitochondrial, Glutaredoxins, Glycerol, Iron-Sulfur Proteins, Schizosaccharomyces pombe Proteins.
- genetics : Schizosaccharomyces.
- growth & development : Schizosaccharomyces.
- metabolism : Mitochondria, Schizosaccharomyces.
Abstract
Mitochondrial monothiol glutaredoxins that bind Fe-S cluster are known to participate in Fe-S cluster assembly. However, their precise role has not been well understood. Among three monothiol glutaredoxins (Grx3, 4, and 5) in Schizosaccharomyces pombe only Grx5 resides in mitochondria. The Deltagrx5 mutant requires cysteine on minimal media, and does not grow on non-fermentable carbon source such as glycerol. We found that the mutant is low in the activity of Fe-S enzymes in mitochondria as well as in the cytoplasm. Screening of multi-copy suppressor of growth defects of the mutant identified isa1(+) gene encoding a putative A-type Fe-S scaffold, in addition to mas5(+) and hsc1(+) genes encoding putative chaperones for Fe-S assembly process. Examination of other scaffold and chaperone genes revealed that isa2(+), but not isu1(+) and ssc1(+), complemented the growth phenotype of Deltagrx5 mutant as isa1(+) did, partly through restoration of Fe-S enzyme activities. The mutant also showed a significant decrease in the amount of mitochondrial DNA. We demonstrated that Grx5 interacts in vivo with Isa1 and Isa2 proteins in mitochondria by observing bimolecular fluorescence complementation. These results indicate that Grx5 plays a central role in Fe-S assembly process through interaction with A-type Fe-S scaffold proteins Isa1 and Isa2, each of which is an essential protein in S. pombe, and supports mitochondrial genome integrity as well as Fe-S assembly.
DOI: 10.1016/j.bbrc.2010.01.051
PubMed: 20085751
Affiliations:
Links toward previous steps (curation, corpus...)
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type="city">Séoul</settlement></placeName></affiliation></author><author><name sortKey="Chung, Woo Hyun" sort="Chung, Woo Hyun" uniqKey="Chung W" first="Woo-Hyun" last="Chung">Woo-Hyun Chung</name></author><author><name sortKey="Kim, Hyo Jin" sort="Kim, Hyo Jin" uniqKey="Kim H" first="Hyo-Jin" last="Kim">Hyo-Jin Kim</name></author><author><name sortKey="Lee, Kyung Chang" sort="Lee, Kyung Chang" uniqKey="Lee K" first="Kyung-Chang" last="Lee">Kyung-Chang Lee</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="eISSN">1090-2104</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cysteine (metabolism)</term><term>DNA, Mitochondrial (metabolism)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Glycerol (metabolism)</term><term>Iron-Sulfur Proteins (genetics)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Mitochondria (metabolism)</term><term>Schizosaccharomyces (genetics)</term><term>Schizosaccharomyces (growth & development)</term><term>Schizosaccharomyces (metabolism)</term><term>Schizosaccharomyces pombe Proteins (genetics)</term><term>Schizosaccharomyces pombe Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN mitochondrial (métabolisme)</term><term>Cystéine (métabolisme)</term><term>Ferrosulfoprotéines (génétique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glycérol (métabolisme)</term><term>Mitochondries (métabolisme)</term><term>Protéines de Schizosaccharomyces pombe (génétique)</term><term>Protéines de Schizosaccharomyces pombe (métabolisme)</term><term>Schizosaccharomyces (croissance et développement)</term><term>Schizosaccharomyces (génétique)</term><term>Schizosaccharomyces (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Iron-Sulfur Proteins</term><term>Schizosaccharomyces pombe Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term><term>DNA, Mitochondrial</term><term>Glutaredoxins</term><term>Glycerol</term><term>Iron-Sulfur Proteins</term><term>Schizosaccharomyces pombe Proteins</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Glutarédoxines</term><term>Protéines de Schizosaccharomyces pombe</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN mitochondrial</term><term>Cystéine</term><term>Ferrosulfoprotéines</term><term>Glutarédoxines</term><term>Glycérol</term><term>Mitochondries</term><term>Protéines de Schizosaccharomyces pombe</term><term>Schizosaccharomyces</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mitochondrial monothiol glutaredoxins that bind Fe-S cluster are known to participate in Fe-S cluster assembly. However, their precise role has not been well understood. Among three monothiol glutaredoxins (Grx3, 4, and 5) in Schizosaccharomyces pombe only Grx5 resides in mitochondria. The Deltagrx5 mutant requires cysteine on minimal media, and does not grow on non-fermentable carbon source such as glycerol. We found that the mutant is low in the activity of Fe-S enzymes in mitochondria as well as in the cytoplasm. Screening of multi-copy suppressor of growth defects of the mutant identified isa1(+) gene encoding a putative A-type Fe-S scaffold, in addition to mas5(+) and hsc1(+) genes encoding putative chaperones for Fe-S assembly process. Examination of other scaffold and chaperone genes revealed that isa2(+), but not isu1(+) and ssc1(+), complemented the growth phenotype of Deltagrx5 mutant as isa1(+) did, partly through restoration of Fe-S enzyme activities. The mutant also showed a significant decrease in the amount of mitochondrial DNA. We demonstrated that Grx5 interacts in vivo with Isa1 and Isa2 proteins in mitochondria by observing bimolecular fluorescence complementation. These results indicate that Grx5 plays a central role in Fe-S assembly process through interaction with A-type Fe-S scaffold proteins Isa1 and Isa2, each of which is an essential protein in S. pombe, and supports mitochondrial genome integrity as well as Fe-S assembly.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20085751</PMID><DateCompleted><Year>2010</Year><Month>03</Month><Day>23</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>392</Volume><Issue>3</Issue><PubDate><Year>2010</Year><Month>Feb</Month><Day>12</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast.</ArticleTitle><Pagination><MedlinePgn>467-72</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2010.01.051</ELocationID><Abstract><AbstractText>Mitochondrial monothiol glutaredoxins that bind Fe-S cluster are known to participate in Fe-S cluster assembly. However, their precise role has not been well understood. Among three monothiol glutaredoxins (Grx3, 4, and 5) in Schizosaccharomyces pombe only Grx5 resides in mitochondria. The Deltagrx5 mutant requires cysteine on minimal media, and does not grow on non-fermentable carbon source such as glycerol. We found that the mutant is low in the activity of Fe-S enzymes in mitochondria as well as in the cytoplasm. Screening of multi-copy suppressor of growth defects of the mutant identified isa1(+) gene encoding a putative A-type Fe-S scaffold, in addition to mas5(+) and hsc1(+) genes encoding putative chaperones for Fe-S assembly process. Examination of other scaffold and chaperone genes revealed that isa2(+), but not isu1(+) and ssc1(+), complemented the growth phenotype of Deltagrx5 mutant as isa1(+) did, partly through restoration of Fe-S enzyme activities. The mutant also showed a significant decrease in the amount of mitochondrial DNA. We demonstrated that Grx5 interacts in vivo with Isa1 and Isa2 proteins in mitochondria by observing bimolecular fluorescence complementation. These results indicate that Grx5 plays a central role in Fe-S assembly process through interaction with A-type Fe-S scaffold proteins Isa1 and Isa2, each of which is an essential protein in S. pombe, and supports mitochondrial genome integrity as well as Fe-S assembly.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Kyoung-Dong</ForeName><Initials>KD</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Seoul National University, Seoul 151-742, South Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chung</LastName><ForeName>Woo-Hyun</ForeName><Initials>WH</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Hyo-Jin</ForeName><Initials>HJ</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Kyung-Chang</ForeName><Initials>KC</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><ArticleDate DateType="Electronic"><Year>2010</Year><Month>01</Month><Day>18</Day></ArticleDate></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="D004272">DNA, Mitochondrial</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C547960">Grx5 protein, S 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004272" MajorTopicYN="N">DNA, Mitochondrial</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</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="D005990" MajorTopicYN="N">Glycerol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName 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PubStatus="entrez"><Year>2010</Year><Month>1</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>1</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>3</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20085751</ArticleId><ArticleId IdType="pii">S0006-291X(10)00089-6</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2010.01.051</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="Chung, Woo Hyun" sort="Chung, Woo Hyun" uniqKey="Chung W" first="Woo-Hyun" last="Chung">Woo-Hyun Chung</name><name sortKey="Kim, Hyo Jin" sort="Kim, Hyo Jin" uniqKey="Kim H" first="Hyo-Jin" last="Kim">Hyo-Jin Kim</name><name sortKey="Lee, Kyung Chang" sort="Lee, Kyung Chang" uniqKey="Lee K" first="Kyung-Chang" last="Lee">Kyung-Chang Lee</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="Kim, Kyoung Dong" sort="Kim, Kyoung Dong" uniqKey="Kim K" first="Kyoung-Dong" last="Kim">Kyoung-Dong Kim</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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