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Artículo

Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193

Randall, Lía M.; Dalla Rizza, Joaquín; Parsonage, Derek; Santos, JavierIcon ; Mehl, Ryan A.; Lowther, W. Todd; Poole, Leslie B.; Denicola, Ana
Fecha de publicación: 09/2019
Editorial: Elsevier Science Inc.
Revista: Free Radical Biology and Medicine
ISSN: 0891-5849
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Bioquímica y Biología Molecular

Resumen

Peroxiredoxins (Prx) are enzymes that efficiently reduce hydroperoxides through active participation of cysteine residues (CP, CR). The first step in catalysis, the reduction of peroxide substrate, is fast, 107 - 108 M−1s−1 for human Prx2. In addition, the high intracellular concentration of Prx positions them not only as good antioxidants but also as central players in redox signaling pathways. These biological functions can be affected by post-translational modifications that could alter the peroxidase activity and/or interaction with other proteins. In particular, inactivation by hyperoxidation of CP, which occurs when a second molecule of peroxide reacts with the CP in the sulfenic acid form, modulates their participation in redox signaling pathways. The higher sensitivity to hyperoxidation of some Prx has been related to the presence of structural motifs that disfavor disulfide formation at the active site, making the CP sulfenic acid more available for hyperoxidation or interaction with a redox protein target. We previously reported that treatment of human Prx2 with peroxynitrite results in tyrosine nitration, a post-translational modification on non-catalytic residues, yielding a more active peroxidase with higher resistance to hyperoxidation. In this work, studies on various mutants of hPrx2 confirm that the presence of the tyrosyl side-chain of Y193, belonging to the C-terminal YF motif of eukaryotic Prx, is necessary to observe the increase in Prx2 resistance to hyperoxidation. Moreover, our results underline the critical role of this structural motif on the rate of disulfide formation that determines the differential participation of Prx in redox signaling pathways.
Palabras clave: HYDROGEN PEROXIDE , HYPEROXIDATION , OXIDATIVE STRESS , PEROXIREDOXIN , PEROXYNITRITE , POST‐TRANSLATIONAL MODIFICATION (PTM) , REDOX SIGNALING , TYROSINE NITRATION
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Atribución-NoComercial-SinDerivadas 2.5 Argentina (CC BY-NC-ND 2.5 AR)
Identificadores
URI: http://hdl.handle.net/11336/162440
URL: https://linkinghub.elsevier.com/retrieve/pii/S0891584919304629
DOI: http://dx.doi.org/10.1016/j.freeradbiomed.2019.07.016
Colecciones
Articulos(IQUIFIB)
Articulos de INST.DE QUIMICA Y FISICO-QUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Articulos(OCA CIUDAD UNIVERSITARIA)
Articulos de OFICINA DE COORDINACION ADMINISTRATIVA CIUDAD UNIVERSITARIA
Citación
Randall, Lía M.; Dalla Rizza, Joaquín; Parsonage, Derek; Santos, Javier; Mehl, Ryan A.; et al.; Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193; Elsevier Science Inc.; Free Radical Biology and Medicine; 141; 9-2019; 492-501
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