Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms

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dc.contributor.authorTairum, Carlos A. [UNESP]
dc.contributor.authorSantos, Melina Cardoso [UNESP]
dc.contributor.authorBreyer, Carlos A. [UNESP]
dc.contributor.authorRyan Geyer, R.
dc.contributor.authorNieves, Cecilia J.
dc.contributor.authorPortillo-Ledesma, Stephanie
dc.contributor.authorFerrer-Sueta, Gerardo
dc.contributor.authorToledo, Jose Carlos
dc.contributor.authorToyama, Marcos H. [UNESP]
dc.contributor.authorAugusto, Ohara
dc.contributor.authorNetto, Luis E. S.
dc.contributor.authorOliveira, Marcos A. de [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniv Republ Montevideo
dc.date.accessioned2018-11-26T17:06:07Z
dc.date.available2018-11-26T17:06:07Z
dc.date.issued2016-09-15
dc.description.abstractTypical 2-Cys Peroxiredoxins (2-Cys Prxs) reduce hydroperoxides with extraordinary rates due to an active site composed of a catalytic triad, containing a peroxidatic cysteine (CP), an Arg, and a Thr (or Ser). 2-Cys Prx are involved in processes such as cancer; neurodegeneration and host-pathogen interactions. During catalysis, 2-Cys Prxs switch between decamers and dimers. Analysis of 2-Cys Prx structures in the fully folded (but not locally unfolded) form revealed a highly conserved, non-conventional hydrogen bond (CH-p) between the catalytic triad Thr of a dimer with an aromatic residue of an adjacent dimer. In contrast, structures of 2-Cys Prxs with a Ser in place of the Thr do not display this CH-p bond. Chromatographic and structural data indicate that the Thr (but not Ser) destabilizes the decamer structure in the oxidized state probably through steric hindrance. As a general trend, mutations in a yeast 2-Cys Prx (Tsa1) favoring the dimeric state also displayed a decreased catalytic activity. Remarkably, yeast naturally contains Thr-Ser variants (Tsa1 and Tsa2, respectively) with distinct oligomeric stabilities in their disulfide states.en
dc.description.affiliationUniv Estadual Paulista, Inst Biociencias, Campus Litoral Paulista, BR-11330900 Sao Paulo, Brazil
dc.description.affiliationUniv Sao Paulo, Inst Quim, Dept Bioquim, BR-05508090 Sao Paulo, Brazil
dc.description.affiliationUniv Republ Montevideo, Fac Ciencias, Montevideo, Uruguay
dc.description.affiliationUniv Sao Paulo, Dept Quim, Fac Filosofia Ciencias & Letras Ribeirao Preto, BR-14040901 Ribeirao Preto, SP, Brazil
dc.description.affiliationUniv Sao Paulo, Inst Biociencias, Dept Genet & Biol Evolut, BR-05508090 Sao Paulo, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Biociencias, Campus Litoral Paulista, BR-11330900 Sao Paulo, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdFAPESP: 07/50930-3
dc.description.sponsorshipIdFAPESP: 13/07937-8
dc.format.extent12
dc.identifierhttp://dx.doi.org/10.1038/srep33133
dc.identifier.citationScientific Reports. London: Nature Publishing Group, v. 6, 12 p., 2016.
dc.identifier.doi10.1038/srep33133
dc.identifier.fileWOS000383191900001.pdf
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/11449/161906
dc.identifier.wosWOS:000383191900001
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofScientific Reports
dc.relation.ispartofsjr1,533
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.titleCatalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanismsen
dc.typeArtigo
dcterms.rightsHolderNature Publishing Group
unesp.author.orcid0000-0002-7220-4286[10]

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