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S-nitrosylation/denitrosylation as a regulatory mechanism of salt stress sensing in sunflower seedlings.
Physiol Plant. 2018 Jan; 162(1):49-72.PP

Abstract

Nitric oxide (NO) and various reactive nitrogen species produced in cells in normal growth conditions, and their enhanced production under stress conditions are responsible for a variety of biochemical aberrations. The present findings demonstrate that sunflower seedling roots exhibit high sensitivity to salt stress in terms of nitrite accumulation. A significant reduction in S-nitrosoglutathione reductase (GSNOR) activity is evident in response to salt stress. Restoration of GSNOR activity with dithioerythritol shows that the enzyme is reversibly inhibited under conditions of 120 mM NaCl. Salt stress-mediated S-nitrosylation of cytosolic proteins was analyzed in roots and cotyledons using biotin-switch assay. LC-MS/MS analysis revealed opposite patterns of S-nitrosylation in seedling cotyledons and roots. Salt stress enhances S-nitrosylation of proteins in cotyledons, whereas roots exhibit denitrosylation of proteins. Highest number of proteins having undergone S-nitrosylation belonged to the category of carbohydrate metabolism followed by other metabolic proteins. Of the total 61 proteins observed to be regulated by S-nitrosylation, 17 are unique to cotyledons, 4 are unique to roots whereas 40 are common to both. Eighteen S-nitrosylated proteins are being reported for the first time in plant systems, including pectinesterase, phospholipase d-alpha and calmodulin. Further physiological analysis of glyceraldehyde-3-phosphate dehydrogenase and monodehydroascorbate reductase showed that salt stress leads to a reversible inhibition of both these enzymes in cotyledons. However, seedling roots exhibit enhanced enzyme activity under salinity stress. These observations implicate the role of S-nitrosylation and denitrosylation in NO signaling thereby regulating various enzyme activities under salinity stress in sunflower seedlings.

Authors+Show Affiliations

Laboratory of Plant Physiology and Biochemistry, Department of Botany, University of Delhi, Delhi 110007, India.Research Unit Protein Science, Helmholtz Zentrum Muenchen, D-80939, München, Germany.Helmholtz Zentrum Muenchen, German Research Center for Environmental Health, Neuherberg, Germany.Laboratory of Plant Physiology and Biochemistry, Department of Botany, University of Delhi, Delhi 110007, India.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28902403

Citation

Jain, Prachi, et al. "S-nitrosylation/denitrosylation as a Regulatory Mechanism of Salt Stress Sensing in Sunflower Seedlings." Physiologia Plantarum, vol. 162, no. 1, 2018, pp. 49-72.
Jain P, von Toerne C, Lindermayr C, et al. S-nitrosylation/denitrosylation as a regulatory mechanism of salt stress sensing in sunflower seedlings. Physiol Plant. 2018;162(1):49-72.
Jain, P., von Toerne, C., Lindermayr, C., & Bhatla, S. C. (2018). S-nitrosylation/denitrosylation as a regulatory mechanism of salt stress sensing in sunflower seedlings. Physiologia Plantarum, 162(1), 49-72. https://doi.org/10.1111/ppl.12641
Jain P, et al. S-nitrosylation/denitrosylation as a Regulatory Mechanism of Salt Stress Sensing in Sunflower Seedlings. Physiol Plant. 2018;162(1):49-72. PubMed PMID: 28902403.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - S-nitrosylation/denitrosylation as a regulatory mechanism of salt stress sensing in sunflower seedlings. AU - Jain,Prachi, AU - von Toerne,Christine, AU - Lindermayr,Christian, AU - Bhatla,Satish C, Y1 - 2017/10/26/ PY - 2017/06/09/received PY - 2017/08/31/revised PY - 2017/09/06/accepted PY - 2017/9/14/pubmed PY - 2018/7/24/medline PY - 2017/9/14/entrez SP - 49 EP - 72 JF - Physiologia plantarum JO - Physiol Plant VL - 162 IS - 1 N2 - Nitric oxide (NO) and various reactive nitrogen species produced in cells in normal growth conditions, and their enhanced production under stress conditions are responsible for a variety of biochemical aberrations. The present findings demonstrate that sunflower seedling roots exhibit high sensitivity to salt stress in terms of nitrite accumulation. A significant reduction in S-nitrosoglutathione reductase (GSNOR) activity is evident in response to salt stress. Restoration of GSNOR activity with dithioerythritol shows that the enzyme is reversibly inhibited under conditions of 120 mM NaCl. Salt stress-mediated S-nitrosylation of cytosolic proteins was analyzed in roots and cotyledons using biotin-switch assay. LC-MS/MS analysis revealed opposite patterns of S-nitrosylation in seedling cotyledons and roots. Salt stress enhances S-nitrosylation of proteins in cotyledons, whereas roots exhibit denitrosylation of proteins. Highest number of proteins having undergone S-nitrosylation belonged to the category of carbohydrate metabolism followed by other metabolic proteins. Of the total 61 proteins observed to be regulated by S-nitrosylation, 17 are unique to cotyledons, 4 are unique to roots whereas 40 are common to both. Eighteen S-nitrosylated proteins are being reported for the first time in plant systems, including pectinesterase, phospholipase d-alpha and calmodulin. Further physiological analysis of glyceraldehyde-3-phosphate dehydrogenase and monodehydroascorbate reductase showed that salt stress leads to a reversible inhibition of both these enzymes in cotyledons. However, seedling roots exhibit enhanced enzyme activity under salinity stress. These observations implicate the role of S-nitrosylation and denitrosylation in NO signaling thereby regulating various enzyme activities under salinity stress in sunflower seedlings. SN - 1399-3054 UR - https://www.unboundmedicine.com/medline/citation/28902403/S_nitrosylation/denitrosylation_as_a_regulatory_mechanism_of_salt_stress_sensing_in_sunflower_seedlings_ DB - PRIME DP - Unbound Medicine ER -