The iron uptake repressor Fep1 in the fission yeast binds Fe-S cluster through conserved cysteines.
Identifieur interne : 000404 ( Main/Exploration ); précédent : 000403; suivant : 000405The iron uptake repressor Fep1 in the fission yeast binds Fe-S cluster through conserved cysteines.
Auteurs : Hyo-Jin Kim [Corée du Sud] ; Kang-Lok Lee [Corée du Sud] ; Kyoung-Dong Kim [Corée du Sud] ; Jung-Hye Roe [Corée du Sud]Source :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2016.
Descripteurs français
- KwdFr :
- Cystéine (composition chimique), Facteurs de transcription GATA (composition chimique), Fer (MeSH), Ferrosulfoprotéines (composition chimique), Liaison aux protéines (MeSH), Protéines de Schizosaccharomyces pombe (composition chimique), Schizosaccharomyces (composition chimique), Sites de fixation (MeSH), Séquence conservée (MeSH).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Cysteine, GATA Transcription Factors, Iron-Sulfur Proteins, Schizosaccharomyces pombe Proteins.
- chemistry : Schizosaccharomyces.
- Binding Sites, Conserved Sequence, Iron, Protein Binding.
Abstract
Iron homeostasis is tightly regulated since iron is an essential but toxic element in the cell. The GATA-type transcription factor Fep1 and its orthologs contribute to iron homeostasis in many fungi by repressing genes for iron uptake when intracellular iron is high. Even though the function and interaction partners of Fep1 have been elucidated extensively In Schizosaccharomyces pombe, the mechanism behind iron-sensing by Fep1 remains elusive. It has been reported that Fep1 interacts with Fe-S-containing monothiol glutaredoxin Grx4 and Grx4-Fra2 complex. In this study, we demonstrate that Fep1 also binds iron, in the form of Fe-S cluster. Spectroscopic and biochemical analyses of as isolated and reconstituted Fep1 suggest that the dimeric Fep1 binds Fe-S clusters. The mutation study revealed that the cluster-binding depended on the conserved cysteines located between the two zinc fingers in the DNA binding domain. EPR analyses revealed [Fe-S]-specific peaks indicative of mixed presence of [2Fe-2S], [3Fe-4S], or [4Fe-4S]. The finding that Fep1 is an Fe-S protein fits nicely with the model that the Fe-S-trafficking Grx4 senses intracellular iron environment and modulates the activity of Fep1.
DOI: 10.1016/j.bbrc.2016.07.070
PubMed: 27444384
Affiliations:
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Electronic address: jhroe@snu.ac.kr.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>School of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 151-742</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName><placeName><settlement type="city">Séoul</settlement></placeName></affiliation></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term><term>Conserved Sequence (MeSH)</term><term>Cysteine (chemistry)</term><term>GATA Transcription Factors (chemistry)</term><term>Iron (MeSH)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Protein Binding (MeSH)</term><term>Schizosaccharomyces (chemistry)</term><term>Schizosaccharomyces pombe Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cystéine (composition chimique)</term><term>Facteurs de transcription GATA (composition chimique)</term><term>Fer (MeSH)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Liaison aux protéines (MeSH)</term><term>Protéines de Schizosaccharomyces pombe (composition chimique)</term><term>Schizosaccharomyces (composition chimique)</term><term>Sites de fixation (MeSH)</term><term>Séquence conservée (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>GATA Transcription Factors</term><term>Iron-Sulfur Proteins</term><term>Schizosaccharomyces pombe Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Facteurs de transcription GATA</term><term>Ferrosulfoprotéines</term><term>Protéines de Schizosaccharomyces pombe</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Conserved Sequence</term><term>Iron</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Fer</term><term>Liaison aux protéines</term><term>Sites de fixation</term><term>Séquence conservée</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Iron homeostasis is tightly regulated since iron is an essential but toxic element in the cell. The GATA-type transcription factor Fep1 and its orthologs contribute to iron homeostasis in many fungi by repressing genes for iron uptake when intracellular iron is high. Even though the function and interaction partners of Fep1 have been elucidated extensively In Schizosaccharomyces pombe, the mechanism behind iron-sensing by Fep1 remains elusive. It has been reported that Fep1 interacts with Fe-S-containing monothiol glutaredoxin Grx4 and Grx4-Fra2 complex. In this study, we demonstrate that Fep1 also binds iron, in the form of Fe-S cluster. Spectroscopic and biochemical analyses of as isolated and reconstituted Fep1 suggest that the dimeric Fep1 binds Fe-S clusters. The mutation study revealed that the cluster-binding depended on the conserved cysteines located between the two zinc fingers in the DNA binding domain. EPR analyses revealed [Fe-S]-specific peaks indicative of mixed presence of [2Fe-2S], [3Fe-4S], or [4Fe-4S]. The finding that Fep1 is an Fe-S protein fits nicely with the model that the Fe-S-trafficking Grx4 senses intracellular iron environment and modulates the activity of Fep1.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27444384</PMID><DateCompleted><Year>2017</Year><Month>05</Month><Day>23</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>478</Volume><Issue>1</Issue><PubDate><Year>2016</Year><Month>09</Month><Day>09</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>The iron uptake repressor Fep1 in the fission yeast binds Fe-S cluster through conserved cysteines.</ArticleTitle><Pagination><MedlinePgn>187-192</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0006-291X(16)31192-5</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2016.07.070</ELocationID><Abstract><AbstractText>Iron homeostasis is tightly regulated since iron is an essential but toxic element in the cell. The GATA-type transcription factor Fep1 and its orthologs contribute to iron homeostasis in many fungi by repressing genes for iron uptake when intracellular iron is high. Even though the function and interaction partners of Fep1 have been elucidated extensively In Schizosaccharomyces pombe, the mechanism behind iron-sensing by Fep1 remains elusive. It has been reported that Fep1 interacts with Fe-S-containing monothiol glutaredoxin Grx4 and Grx4-Fra2 complex. In this study, we demonstrate that Fep1 also binds iron, in the form of Fe-S cluster. Spectroscopic and biochemical analyses of as isolated and reconstituted Fep1 suggest that the dimeric Fep1 binds Fe-S clusters. The mutation study revealed that the cluster-binding depended on the conserved cysteines located between the two zinc fingers in the DNA binding domain. EPR analyses revealed [Fe-S]-specific peaks indicative of mixed presence of [2Fe-2S], [3Fe-4S], or [4Fe-4S]. The finding that Fep1 is an Fe-S protein fits nicely with the model that the Fe-S-trafficking Grx4 senses intracellular iron environment and modulates the activity of Fep1.</AbstractText><CopyrightInformation>Copyright © 2016 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Hyo-Jin</ForeName><Initials>HJ</Initials><AffiliationInfo><Affiliation>School of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Kang-Lok</ForeName><Initials>KL</Initials><AffiliationInfo><Affiliation>School of Biological Sciences and 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><AffiliationInfo><Affiliation>School of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Roe</LastName><ForeName>Jung-Hye</ForeName><Initials>JH</Initials><AffiliationInfo><Affiliation>School of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea. Electronic address: jhroe@snu.ac.kr.</Affiliation></AffiliationInfo></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>2016</Year><Month>07</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="C459859">Fep1 protein, S pombe</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050980">GATA Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029702">Schizosaccharomyces pombe Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050980" MajorTopicYN="N">GATA Transcription Factors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029702" MajorTopicYN="N">Schizosaccharomyces pombe Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">EPR</Keyword><Keyword MajorTopicYN="Y">Fe-S</Keyword><Keyword MajorTopicYN="Y">Fission yeast</Keyword><Keyword MajorTopicYN="Y">Glutaredoxin</Keyword><Keyword MajorTopicYN="Y">Iron homeostasis</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>07</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>07</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>7</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>7</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>5</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27444384</ArticleId><ArticleId IdType="pii">S0006-291X(16)31192-5</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2016.07.070</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><country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Kim, Hyo Jin" sort="Kim, Hyo Jin" uniqKey="Kim H" first="Hyo-Jin" last="Kim">Hyo-Jin Kim</name></region><name sortKey="Kim, Kyoung Dong" sort="Kim, Kyoung Dong" uniqKey="Kim K" first="Kyoung-Dong" last="Kim">Kyoung-Dong Kim</name><name sortKey="Lee, Kang Lok" sort="Lee, Kang Lok" uniqKey="Lee K" first="Kang-Lok" last="Lee">Kang-Lok Lee</name><name sortKey="Roe, Jung Hye" sort="Roe, Jung Hye" uniqKey="Roe J" first="Jung-Hye" last="Roe">Jung-Hye Roe</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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