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Erratum for Chaki et al., Plant Cell Physiol. 50 (2) 265-279.
Plant and Cell Physiology 2009 50(3):665-679; doi:10.1093/pcp/pcp039
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© The Author 2008. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Erratum

Involvement of Reactive Nitrogen and Oxygen Species (RNS and ROS) in Sunflower–Mildew Interaction

Mounira Chaki1, Ana M. Fernández-Ocaña1, Raquel Valderrama1, Alfonso Carreras1, Francisco J. Esteban1, Francisco Luque1, María V. Gómez-Rodríguez1, Juan C. Begara-Morales1, Francisco J. Corpas2,* and Juan B. Barroso1

1Grupo de Señalización Molecular y Sistemas Antioxidantes en Plantas, Unidad Asociada al CSIC (EEZ), Departamento de Bioquímica, y Biología Molecular, Universidad de Jaén, Spain
2Departamento de Bioquímica, Biología Celular y Molecular de Plantas, Estación Experimental del Zaidín, CSIC, Granada, Spain

*Corresponding author: E-mail, javier.corpas{at}eez.csic.es; Fax, +34-958-129600.

Abstract


  Abstract

Nitric oxide (·NO) has been shown to participate in plant response against pathogen infection; however, less is known of the participation of other NO-derived molecules designated as reactive nitrogen species (RNS). Using two sunflower (Helianthus annuus L.) cultivars with different sensitivity to infection by the pathogen Plasmopara halstedii, we studied key components involved in RNS and ROS metabolism. We analyzed the superoxide radical production, hydrogen peroxide content, L-arginine-dependent nitric oxide synthase (NOS) and S-nitrosoglutathione reductase (GSNOR) activities. Furthermore, we examined the location and contents of ·NO, S-nitrosothiols (RSNOs), S-nitrosoglutathione (GSNO) and protein 3-nitrotyrosine (NO2-Tyr) by confocal laser scanning microscopy (CLSM) and biochemical analyses. In the susceptible cultivar, the pathogen induces an increase in proteins that undergo tyrosine nitration accompanied by an augmentation in RSNOs. This rise of RSNOs seems to be independent of the enzymatic generation of ·NO because the L-arginine-dependent NOS activity is reduced after infection. These results suggest that pathogens induce nitrosative stress in susceptible cultivars. In contrast, in the resistant cultivar, no increase of RSNOs or tyrosine nitration of proteins was observed, implying an absence of nitrosative stress. Therefore, it is proposed that the increase of tyrosine nitration of proteins can be considered a general biological marker of nitrosative stress in plants under biotic conditions.

Keywords: Nitric oxide - Nitric oxide synthase - Nitrosative stress - Nitrotyrosine - Reactive nitrogen species (RNS) - S-Nitrosoglutathione reductase.

Abbreviations: BSA, bovine serum albumin;; CLSM, confocal laser scanning microscopy;; cPTIO, 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide;; DAF-2 DA, 4,5-diaminoflorescein diacetate;; DHE, dihydroethidium;; dpi, days post-infection;; DTT, dithiothreitol;; GSNO, S-nitrosoglutathione;; GSNOR, S-nitrosoglutathione reductase;; HR, hypersensitive response;; NEM, N-ethylmaleimide;; NO, nitric oxide;; NO2-Tyr, 3-nitrotyrosine;; NOS, nitric oxide synthase;; PBS, phosphate-buffered saline;; PMSF, phenylmethylsulfonyl fluoride;; PVPP, polyvinyl polypyrrol-idone;; RNS, reactive nitrogen species;; ROS, reactive oxygen species;; RSNO, S-nitrosothiol;; RT–PCR, reverse transcription–PCR;; TMP, 2,2,6,6-tetramethyl-piperidine.

(Received December 2, 2008; Accepted December 12, 2008)
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