A New Class of Thioredoxin-Related Protein Able to Bind Iron-Sulfur Clusters.
Identifieur interne : 000481 ( Main/Exploration ); précédent : 000480; suivant : 000482A New Class of Thioredoxin-Related Protein Able to Bind Iron-Sulfur Clusters.
Auteurs : Hugo Bisio [Uruguay] ; Mariana Bonilla [Uruguay] ; Bruno Manta [Uruguay] ; Martín Gra A [Uruguay] ; Valentina Salzman [Uruguay] ; Pablo S. Aguilar [Uruguay] ; Vadim N. Gladyshev [États-Unis] ; Marcelo A. Comini [Uruguay] ; Gustavo Salinas [Uruguay]Source :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2016.
Abstract
AIMS
Members of the thioredoxin (Trx) protein family participate mainly in redox pathways and have not been associated with Fe/S binding, in contrast to some closely related glutaredoxins (Grxs). Cestode parasites possess an unusual diversity of Trxs and Trx-related proteins with unexplored functions. In this study, we addressed the biochemical characterization of a new class of Trx-related protein (IsTRP) and a classical monothiol Grx (EgGrx5) from the human pathogen Echinococcus granulosus.
RESULTS
The dimeric form of IsTRP coordinates Fe
INNOVATION
IsTRP is the first member from the Trx family to be reported to bind Fe/S. We disclose a novel mechanism of Fe/S coordination within the Trx folding unit, which renders the cluster highly resistant to oxidation-mediated disassembly.
CONCLUSION
We demonstrate that IsTRP defines a new protein family within the Trx superfamily, confirm the conservation of function for class II Grx from nonphylogenetically related species, and highlight the versatility of the Trx folding unit to acquire Fe/S binding as a recurrent emergent function. Antioxid. Redox Signal. 00, 000-000.
DOI: 10.1089/ars.2015.6377
PubMed: 26381228
PubMed Central: PMC6913166
Affiliations:
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Aguilar</name><affiliation wicri:level="1"><nlm:affiliation>4 Cellular Membranes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>4 Cellular Membranes Laboratory, Institut Pasteur de Montevideo , Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation></author><author><name sortKey="Gladyshev, Vadim N" sort="Gladyshev, Vadim N" uniqKey="Gladyshev V" first="Vadim N" last="Gladyshev">Vadim N. Gladyshev</name><affiliation wicri:level="2"><nlm:affiliation>5 Division of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School , Boston, Massachusetts.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>5 Division of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School , Boston</wicri:cityArea></affiliation></author><author><name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name><affiliation wicri:level="1"><nlm:affiliation>2 Redox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>2 Redox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo , Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation></author><author><name sortKey="Salinas, Gustavo" sort="Salinas, Gustavo" uniqKey="Salinas G" first="Gustavo" last="Salinas">Gustavo Salinas</name><affiliation wicri:level="1"><nlm:affiliation>1 Worm Biology Laboratory, Institut Pasteur de Montevideo, Montevideo, Uruguay .</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>1 Worm Biology Laboratory, Institut Pasteur de Montevideo, Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>6 Cátedra de Inmunología, Departamento de Biociencias, Facultad de Química, Universidad de la República , Montevideo, Uruguay .</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>6 Cátedra de Inmunología, Departamento de Biociencias, Facultad de Química, Universidad de la República , Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>AIMS</b></p><p>Members of the thioredoxin (Trx) protein family participate mainly in redox pathways and have not been associated with Fe/S binding, in contrast to some closely related glutaredoxins (Grxs). Cestode parasites possess an unusual diversity of Trxs and Trx-related proteins with unexplored functions. In this study, we addressed the biochemical characterization of a new class of Trx-related protein (IsTRP) and a classical monothiol Grx (EgGrx5) from the human pathogen Echinococcus granulosus.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>The dimeric form of IsTRP coordinates Fe</p></div><div type="abstract" xml:lang="en"><p><b>INNOVATION</b></p><p>IsTRP is the first member from the Trx family to be reported to bind Fe/S. We disclose a novel mechanism of Fe/S coordination within the Trx folding unit, which renders the cluster highly resistant to oxidation-mediated disassembly.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>We demonstrate that IsTRP defines a new protein family within the Trx superfamily, confirm the conservation of function for class II Grx from nonphylogenetically related species, and highlight the versatility of the Trx folding unit to acquire Fe/S binding as a recurrent emergent function. Antioxid. Redox Signal. 00, 000-000.</p></div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">26381228</PMID><DateRevised><Year>2019</Year><Month>12</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>24</Volume><Issue>4</Issue><PubDate><Year>2016</Year><Month>01</Month><Day>27</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>A New Class of Thioredoxin-Related Protein Able to Bind Iron-Sulfur Clusters.</ArticleTitle><Pagination><MedlinePgn>205-216</MedlinePgn></Pagination><Abstract><AbstractText Label="AIMS">Members of the thioredoxin (Trx) protein family participate mainly in redox pathways and have not been associated with Fe/S binding, in contrast to some closely related glutaredoxins (Grxs). Cestode parasites possess an unusual diversity of Trxs and Trx-related proteins with unexplored functions. In this study, we addressed the biochemical characterization of a new class of Trx-related protein (IsTRP) and a classical monothiol Grx (EgGrx5) from the human pathogen Echinococcus granulosus.</AbstractText><AbstractText Label="RESULTS">The dimeric form of IsTRP coordinates Fe<sub>2</sub>S<sub>2</sub> in a glutathione-independent manner; instead, Fe/S binding relies on the CXXC motif conserved among Trxs. This novel binding mechanism allows holo-IsTRP to be highly resistant to oxidation. IsTRP lacks canonical reductase activities. Mitochondrially targeted IsTRP aids growth of a Grx5 null yeast strain. Similar complementation assays performed with EgGrx5 revealed functional conservation for class II Grxs, despite the presence of nonconserved structural elements. IsTRP is a cestode lineage-specific protein highly expressed in the gravid adult worm, which releases the infective stage critical for dissemination.</AbstractText><AbstractText Label="INNOVATION">IsTRP is the first member from the Trx family to be reported to bind Fe/S. We disclose a novel mechanism of Fe/S coordination within the Trx folding unit, which renders the cluster highly resistant to oxidation-mediated disassembly.</AbstractText><AbstractText Label="CONCLUSION">We demonstrate that IsTRP defines a new protein family within the Trx superfamily, confirm the conservation of function for class II Grx from nonphylogenetically related species, and highlight the versatility of the Trx folding unit to acquire Fe/S binding as a recurrent emergent function. Antioxid. Redox Signal. 00, 000-000.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bisio</LastName><ForeName>Hugo</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>1 Worm Biology Laboratory, Institut Pasteur de Montevideo, Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bonilla</LastName><ForeName>Mariana</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>2 Redox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Manta</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>2 Redox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Graña</LastName><ForeName>Martín</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>3 Bioinformatics Unit, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Salzman</LastName><ForeName>Valentina</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>4 Cellular Membranes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aguilar</LastName><ForeName>Pablo S</ForeName><Initials>PS</Initials><AffiliationInfo><Affiliation>4 Cellular Membranes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gladyshev</LastName><ForeName>Vadim N</ForeName><Initials>VN</Initials><AffiliationInfo><Affiliation>5 Division of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School , Boston, Massachusetts.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Comini</LastName><ForeName>Marcelo A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>2 Redox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Salinas</LastName><ForeName>Gustavo</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>1 Worm Biology Laboratory, Institut Pasteur de Montevideo, Montevideo, Uruguay .</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>6 Cátedra de Inmunología, Departamento de Biociencias, Facultad de Química, Universidad de la República , Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R37 GM065204</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>10</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26381228</ArticleId><ArticleId IdType="doi">10.1089/ars.2015.6377</ArticleId><ArticleId IdType="pmc">PMC6913166</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Biol Chem. 2008 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Aguilar</name><name sortKey="Bonilla, Mariana" sort="Bonilla, Mariana" uniqKey="Bonilla M" first="Mariana" last="Bonilla">Mariana Bonilla</name><name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name><name sortKey="Gra A, Martin" sort="Gra A, Martin" uniqKey="Gra A M" first="Martín" last="Gra A">Martín Gra A</name><name sortKey="Manta, Bruno" sort="Manta, Bruno" uniqKey="Manta B" first="Bruno" last="Manta">Bruno Manta</name><name sortKey="Salinas, Gustavo" sort="Salinas, Gustavo" uniqKey="Salinas G" first="Gustavo" last="Salinas">Gustavo Salinas</name><name sortKey="Salinas, Gustavo" sort="Salinas, Gustavo" uniqKey="Salinas G" first="Gustavo" last="Salinas">Gustavo Salinas</name><name sortKey="Salzman, Valentina" sort="Salzman, Valentina" uniqKey="Salzman V" first="Valentina" last="Salzman">Valentina Salzman</name></country><country name="États-Unis"><region name="Massachusetts"><name sortKey="Gladyshev, Vadim N" sort="Gladyshev, Vadim N" uniqKey="Gladyshev V" first="Vadim N" last="Gladyshev">Vadim N. Gladyshev</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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