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dc.contributor.author
Bisio, Hugo
dc.contributor.author
Bonilla, Mariana
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Manta, Bruno
dc.contributor.author
Graña, Juan Martin
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dc.contributor.author
Salzman, Valentina
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Aguilar, Pablo Sebastián
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Gladyshev, Vadim
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Comini, Marcelo
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dc.contributor.author
Salinas, Gustavo
dc.date.available
2018-06-19T18:23:27Z
dc.date.issued
2015-09
dc.identifier.citation
Bisio, Hugo; Bonilla, Mariana; Manta, Bruno; Graña, Juan Martin; Salzman, Valentina; et al.; A New Class of Thioredoxin‐Related Protein Able to Bind Iron-Sulfur Clusters; Mary Ann Liebert; Antioxidants & Redox Signaling; 24; 4; 9-2015; 1-51
dc.identifier.issn
1523-0864
dc.identifier.uri
http://hdl.handle.net/11336/49367
dc.description.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 non-explored functions. Here 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 Fe2S2 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 non-conserved structural elements. IsTRP is a cestode-lineage specific protein highly expressed in the gravid adult worm, which releases the infective stage critical for dissemination.INNOVATION:IsTRP is the first member from the thioredoxin 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 thioredoxin superfamily, confirm the conservation of function for class II glutaredoxin from non-phylogenetically related species and highlight the versatility of the Trx folding unit to acquire Fe/S binding as a recurrent emergent function.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Mary Ann Liebert
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Levaduras
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Redox
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Tioredoxina
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Mitocondria
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Medicina Básica
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dc.subject.classification
CIENCIAS MÉDICAS Y DE LA SALUD
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dc.title
A New Class of Thioredoxin‐Related Protein Able to Bind Iron-Sulfur Clusters
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-06-19T16:53:41Z
dc.journal.volume
24
dc.journal.number
4
dc.journal.pagination
1-51
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Bisio, Hugo. Instituto Pasteur de Montevideo; Uruguay
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Fil: Bonilla, Mariana. Instituto Pasteur de Montevideo; Uruguay
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Fil: Manta, Bruno. Instituto Pasteur de Montevideo; Uruguay
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Fil: Graña, Martin. Instituto Pasteur de Montevideo; Uruguay
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Fil: Salzman, Valentina. Instituto Pasteur de Montevideo; Uruguay. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: Aguilar, Pablo Sebastián. Instituto Pasteur de Montevideo; Uruguay. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: Gladyshev, Vadim. Harvard Medical School; Estados Unidos
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Fil: Comini, Marcelo. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Salinas, Gustavo. Instituto Pasteur de Montevideo; Uruguay. Universidad de la República; Uruguay
dc.journal.title
Antioxidants & Redox Signaling
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.liebertpub.com/doi/10.1089/ars.2015.6377
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1089/ars.2015.6377
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