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Inhibition Of Arabidopsis O-Acetylserine(Thiol)Lyase A1 By Tyrosine-Nitration

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Inhibition Of Arabidopsis O-Acetylserine(Thiol)Lyase A1 By Tyrosine-Nitration

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Nombre: Alvarez;LOZANO;Romero ...
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dc.contributor.author Alvarez, C es_ES
dc.contributor.author Lozano Juste, Jorge es_ES
dc.contributor.author Romero, L.C. es_ES
dc.contributor.author Garcia, I es_ES
dc.contributor.author Gotor, C. es_ES
dc.contributor.author Leon Ramos, Jose es_ES
dc.date.accessioned 2016-07-25T11:48:15Z
dc.date.available 2016-07-25T11:48:15Z
dc.date.issued 2011-06-07
dc.identifier.issn 0021-9258
dc.identifier.uri http://hdl.handle.net/10251/68098
dc.description.abstract The last step of sulfur assimilation is catalyzed by O-acetyl-serine(thiol) lyase (OASTL) enzymes. OASTLs are encoded by a multigene family in the model plant Arabidopsis thaliana. Cytosolic OASA1 enzyme is the main source of OASTL activity and thus crucial for cysteine homeostasis. We found that nitrating conditions after exposure to peroxynitrite strongly inhibited OASTL activity. Among OASTLs, OASA1 was markedly sensitive to nitration as demonstrated by the comparative analysis of OASTL activity in nitrated crude protein extracts from wild type and different oastl mutants. Furthermore, nitration assays on purified recombinant OASA1 protein led to 90% reduction of the activity due to inhibition of the enzyme, as no degradation of the protein occurred under these conditions. The reduced activity was due to nitration of the protein because selective scavenging of peroxynitrite with epicatechin impaired OASA1 nitration and the concomitant inhibition of OASTL activity. Inhibition of OASA1 activity upon nitration correlated with the identification of a modified OASA1 protein containing 3-nitroTyr(302) residue. The essential role of the Tyr(302) residue for the catalytic activity was further demonstrated by the loss of OASTL activity of a Y302A-mutated version of OASA1. Inhibition caused by Tyr(302) nitration on OASA1 activity seems to be due to a drastically reduced O-acetylserine substrate binding to the nitrated protein, and also to reduced stabilization of the pyridoxal-5'-phosphate cofactor through hydrogen bonds. This is the first report identifying a Tyr nitration site of a plant protein with functional effect and the first post-translational modification identified in OASA1 enzyme. es_ES
dc.description.sponsorship This work was supported by Grants BIO2008-00839 and CONSOLIDER TRANSPLANTA CSD2007-00057 (to J. L.) and BIO2010- 15201 (to C. G.). en_EN
dc.language Inglés es_ES
dc.publisher American Society for Biochemistry and Molecular Biology es_ES
dc.relation.ispartof Journal of Biological Chemistry es_ES
dc.rights Reserva de todos los derechos es_ES
dc.title Inhibition Of Arabidopsis O-Acetylserine(Thiol)Lyase A1 By Tyrosine-Nitration es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1074/jbc.M110.147678
dc.relation.projectID info:eu-repo/grantAgreement/MEC//CSD2007-00057/ES/Función y potencial biotecnológico de los factores de transcripción de las plantas./ / es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MICINN//BIO2008-00839/ES/BIOSINTESIS Y FUNCION DEL OXIDO NITRICO EN ARABIDOPSIS. CONEXION CON LOS ACIDOS ABSCISICO, SALICILICO Y JASMONICO/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MICINN//BIO2010-15201/ES/PAPEL FUNCIONAL DE CISTEINA Y S-SULFOCISTEINA EN LA SEÑALIZACION Y CONTROL DE LAS RESPUESTAS DE LAS PLANTAS/ es_ES
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes es_ES
dc.description.bibliographicCitation Alvarez, C.; Lozano Juste, J.; Romero, L.; Garcia, I.; Gotor, C.; Leon Ramos, J. (2011). Inhibition Of Arabidopsis O-Acetylserine(Thiol)Lyase A1 By Tyrosine-Nitration. Journal of Biological Chemistry. 286(1):578-586. doi:10.1074/jbc.M110.147678 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://dx.doi.org/10.1074/jbc.M110.147678 es_ES
dc.description.upvformatpinicio 578 es_ES
dc.description.upvformatpfin 586 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 286 es_ES
dc.description.issue 1 es_ES
dc.relation.senia 213953 es_ES
dc.identifier.pmid 21047785 en_EN
dc.identifier.pmcid PMC3013017 en_EN
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