4.5 Article

Salinity-induced changes in S-nitrosylation of pea mitochondrial proteins

Journal

JOURNAL OF PROTEOMICS
Volume 79, Issue -, Pages 87-99

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.jprot.2012.12.003

Keywords

Mitochondria; Salt stress; S-nitrosylation; Posttranslational modification

Funding

  1. Juan de la Cierva Research program
  2. MICINN [BFU2011-28716, BIO2008-04067]
  3. Seneca Foundation, Murcia, Spain [04553/GERM/06]

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Together with reactive oxygen species, nitric oxide is an essential part of the signal transduction induced by stress conditions. In this work we study the pattern of S-nitrosylated proteins from mitochondria of pea plants subjected to 150 mM NaCl for 5 and 14 days. A differential pattern of target proteins was found during plant development and salt stress, with a minor number of S-nitrosylated proteins at 14 days specifically some key enzymes related to respiration and photorespiration. At this time of stress, only ATP synthase p subunit, peroxiredoxin and Hsp90 were S-nitrosylated and no changes in protein levels were observed, although the activity of PrxII F may be reduced by S-nitrosylation. The NADH/NAD(+) ratio was also high at 14 days but not the NADPH/NADP(+). An enhancement in NO measured by fluorimetry and confocal microscopy was observed in leaves, being part of the NO localized in mitochondria. An increase in mitochondrial GSNOR activity was produced in response to short and long-term NaCl treatment, where a higher number of nitrated proteins were also observed. The results indicated that posttranslational modifications seem to modulate respiratory and photorespiratory pathways, as well as some antioxidant enzymes, through differential S-nitrosylation/denitrosylation in control conditions and under salt stress. (C) 2012 Elsevier B.V. All rights reserved.

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