Cluster exchange reactivity of [2Fe-2S]-bridged heterodimeric BOLA1-GLRX5.
Identifieur interne : 000086 ( Main/Exploration ); précédent : 000085; suivant : 000087Cluster exchange reactivity of [2Fe-2S]-bridged heterodimeric BOLA1-GLRX5.
Auteurs : Sambuddha Sen [États-Unis] ; Amber L. Hendricks [États-Unis] ; James A. Cowan [États-Unis]Source :
- The FEBS journal [ 1742-4658 ] ; 2020.
Abstract
Mitochondrial BOLA1 is known to form a [2Fe-2S] cluster-bridged heterodimeric complex with mitochondrial monothiol glutaredoxin GLRX5; however, the function of this heterodimeric complex is unclear. Some reports suggest redundant roles for BOLA1 and a related protein, BOLA3, with both involved in the maturation of [4Fe-4S] clusters in a subset of mitochondrial proteins. However, a later report on the structure of BOLA1-GLRX5 heterodimeric complex demonstrated a buried cluster environment and predicted a redox role instead of the cluster trafficking role suggested for the BOLA3-GLRX5 heterodimeric complex. Herein, we describe a detailed kinetic study of relative cluster exchange reactivity involving heterodimeric complex of BOLA1 with GLRX5. By the use of CD spectroscopy, it is demonstrated that [2Fe-2S]-bridged BOLA1-GLRX5 can be readily formed by cluster uptake from donors such as ISCU or [2Fe-2S](GS)4 complex, but not from ISCA1 or ISCA2. Rapid holo-formation following delivery from [2Fe-2S](GS)4 supports possible physiological relevance in the cellular labile iron pool. Holo [2Fe-2S] BOLA1-GLRX5 heterodimeric complex is incapable of donating cluster to apo protein acceptors, providing experimental support for a nontrafficking role. Finally, we report the formation and reactivity of the holo [2Fe-2S]-bridged BOLA1 homodimer (lacking a partner GLRX). While the holo-heterodimer is thermodynamically more stable, by contrast the holo BOLA1 homodimer does demonstrate facile cluster exchange reactivity.
DOI: 10.1111/febs.15452
PubMed: 32542995
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Cluster exchange reactivity of [2Fe-2S]-bridged heterodimeric BOLA1-GLRX5.</title><author><name sortKey="Sen, Sambuddha" sort="Sen, Sambuddha" uniqKey="Sen S" first="Sambuddha" last="Sen">Sambuddha Sen</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Hendricks, Amber L" sort="Hendricks, Amber L" uniqKey="Hendricks A" first="Amber L" last="Hendricks">Amber L. Hendricks</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Cowan, James A" sort="Cowan, James A" uniqKey="Cowan J" first="James A" last="Cowan">James A. Cowan</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32542995</idno><idno type="pmid">32542995</idno><idno type="doi">10.1111/febs.15452</idno><idno type="wicri:Area/Main/Corpus">000044</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000044</idno><idno type="wicri:Area/Main/Curation">000044</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000044</idno><idno type="wicri:Area/Main/Exploration">000044</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Cluster exchange reactivity of [2Fe-2S]-bridged heterodimeric BOLA1-GLRX5.</title><author><name sortKey="Sen, Sambuddha" sort="Sen, Sambuddha" uniqKey="Sen S" first="Sambuddha" last="Sen">Sambuddha Sen</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Hendricks, Amber L" sort="Hendricks, Amber L" uniqKey="Hendricks A" first="Amber L" last="Hendricks">Amber L. Hendricks</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Cowan, James A" sort="Cowan, James A" uniqKey="Cowan J" first="James A" last="Cowan">James A. Cowan</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author></analytic><series><title level="j">The FEBS journal</title><idno type="eISSN">1742-4658</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mitochondrial BOLA1 is known to form a [2Fe-2S] cluster-bridged heterodimeric complex with mitochondrial monothiol glutaredoxin GLRX5; however, the function of this heterodimeric complex is unclear. Some reports suggest redundant roles for BOLA1 and a related protein, BOLA3, with both involved in the maturation of [4Fe-4S] clusters in a subset of mitochondrial proteins. However, a later report on the structure of BOLA1-GLRX5 heterodimeric complex demonstrated a buried cluster environment and predicted a redox role instead of the cluster trafficking role suggested for the BOLA3-GLRX5 heterodimeric complex. Herein, we describe a detailed kinetic study of relative cluster exchange reactivity involving heterodimeric complex of BOLA1 with GLRX5. By the use of CD spectroscopy, it is demonstrated that [2Fe-2S]-bridged BOLA1-GLRX5 can be readily formed by cluster uptake from donors such as ISCU or [2Fe-2S](GS)<sub>4</sub> complex, but not from ISCA1 or ISCA2. Rapid holo-formation following delivery from [2Fe-2S](GS)<sub>4</sub> supports possible physiological relevance in the cellular labile iron pool. Holo [2Fe-2S] BOLA1-GLRX5 heterodimeric complex is incapable of donating cluster to apo protein acceptors, providing experimental support for a nontrafficking role. Finally, we report the formation and reactivity of the holo [2Fe-2S]-bridged BOLA1 homodimer (lacking a partner GLRX). While the holo-heterodimer is thermodynamically more stable, by contrast the holo BOLA1 homodimer does demonstrate facile cluster exchange reactivity.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">32542995</PMID><DateRevised><Year>2020</Year><Month>07</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1742-4658</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Jun</Month><Day>15</Day></PubDate></JournalIssue><Title>The FEBS journal</Title><ISOAbbreviation>FEBS J</ISOAbbreviation></Journal><ArticleTitle>Cluster exchange reactivity of [2Fe-2S]-bridged heterodimeric BOLA1-GLRX5.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1111/febs.15452</ELocationID><Abstract><AbstractText>Mitochondrial BOLA1 is known to form a [2Fe-2S] cluster-bridged heterodimeric complex with mitochondrial monothiol glutaredoxin GLRX5; however, the function of this heterodimeric complex is unclear. Some reports suggest redundant roles for BOLA1 and a related protein, BOLA3, with both involved in the maturation of [4Fe-4S] clusters in a subset of mitochondrial proteins. However, a later report on the structure of BOLA1-GLRX5 heterodimeric complex demonstrated a buried cluster environment and predicted a redox role instead of the cluster trafficking role suggested for the BOLA3-GLRX5 heterodimeric complex. Herein, we describe a detailed kinetic study of relative cluster exchange reactivity involving heterodimeric complex of BOLA1 with GLRX5. By the use of CD spectroscopy, it is demonstrated that [2Fe-2S]-bridged BOLA1-GLRX5 can be readily formed by cluster uptake from donors such as ISCU or [2Fe-2S](GS)<sub>4</sub> complex, but not from ISCA1 or ISCA2. Rapid holo-formation following delivery from [2Fe-2S](GS)<sub>4</sub> supports possible physiological relevance in the cellular labile iron pool. Holo [2Fe-2S] BOLA1-GLRX5 heterodimeric complex is incapable of donating cluster to apo protein acceptors, providing experimental support for a nontrafficking role. Finally, we report the formation and reactivity of the holo [2Fe-2S]-bridged BOLA1 homodimer (lacking a partner GLRX). While the holo-heterodimer is thermodynamically more stable, by contrast the holo BOLA1 homodimer does demonstrate facile cluster exchange reactivity.</AbstractText><CopyrightInformation>© 2020 Federation of European Biochemical Societies.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sen</LastName><ForeName>Sambuddha</ForeName><Initials>S</Initials><Identifier Source="ORCID">https://orcid.org/0000-0001-6079-0268</Identifier><AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hendricks</LastName><ForeName>Amber L</ForeName><Initials>AL</Initials><AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cowan</LastName><ForeName>James A</ForeName><Initials>JA</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-4686-6825</Identifier><AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>AI072443</GrantID><Acronym>NH</Acronym><Agency>NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>06</Month><Day>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS J</MedlineTA><NlmUniqueID>101229646</NlmUniqueID><ISSNLinking>1742-464X</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">BOLA</Keyword><Keyword MajorTopicYN="N">GLRX5</Keyword><Keyword MajorTopicYN="N">[2Fe-2S](GS)4 complex</Keyword><Keyword MajorTopicYN="N">glutaredoxin</Keyword><Keyword MajorTopicYN="N">iron-sulfur cluster</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>04</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>06</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>06</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>6</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>6</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>6</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32542995</ArticleId><ArticleId IdType="doi">10.1111/febs.15452</ArticleId></ArticleIdList><ReferenceList><Title>References</Title><Reference><Citation>Santos JM, Freire P, Vicente M & Arraiano CM (1999) The stationary-phase morphogene bolA from Escherichia coli is induced by stress during early stages of growth. 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Biochemistry 52, 6633-6645.</Citation></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Ohio</li></region></list><tree><country name="États-Unis"><region name="Ohio"><name sortKey="Sen, Sambuddha" sort="Sen, Sambuddha" uniqKey="Sen S" first="Sambuddha" last="Sen">Sambuddha Sen</name></region><name sortKey="Cowan, James A" sort="Cowan, James A" uniqKey="Cowan J" first="James A" last="Cowan">James A. Cowan</name><name sortKey="Hendricks, Amber L" sort="Hendricks, Amber L" uniqKey="Hendricks A" first="Amber L" last="Hendricks">Amber L. Hendricks</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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