IngentaConnect S-nitrosylated proteins of a medicinal CAM plant Kalanchoepinnata...

Authors: Abat, Jasmeet K.¹; Mattoo, Autar K.²; Deswal, Renu¹

Source: FEBS Journal, Volume 275, Number 11, June 2008 , pp. 2862-2872(11)

Abstract:

Nitric oxide (NO) is a signaling molecule that affects a myriad of processes in plants. However, the mechanistic details are limited. NO post-translationally modifies proteins by S-nitrosylation of cysteines. The soluble S-nitrosoproteome of a medicinal, crassulacean acid metabolism (CAM) plant, Kalanchoe pinnata, was purified using the biotin switch technique. Nineteen targets were identified by MALDI-TOF mass spectrometry, including proteins associated with carbon, nitrogen and sulfur metabolism, the cytoskeleton, stress and photosynthesis. Some were similar to those previously identified in Arabidopsis thaliana, but kinesin-like protein, glycolate oxidase, putative UDP glucose 4-epimerase and putative DNA topoisomerase II had not been identified as targets previously for any organism. In vitro and in vivo nitrosylation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), one of the targets, was confirmed by immunoblotting. Rubisco plays a central role in photosynthesis, and the effect of S-nitrosylation on its enzymatic activity was determined using NaH¹⁴CO₃. The NO-releasing compound S-nitrosoglutathione inhibited its activity in a dose-dependent manner suggesting Rubisco inactivation by nitrosylation for the first time.

Keywords: biotin switch technique; Kalanchoe pinnata; nitric oxide; Rubisco; S-nitrosylation

Document Type: Research article

DOI: 10.1111/j.1742-4658.2008.06425.x

Affiliations: 1: Department of Botany, Plant Molecular Physiology and Biochemistry Laboratory, University of Delhi, India 2: Sustainable Agricultural Systems Laboratory, The Henry A. Wallace Beltsville Agricultural Research Center, MD, USA

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S-nitrosylated proteins of a medicinal CAM plant Kalanchoe pinnata- ribulose-1,5-bisphosphate carboxylase/oxygenase activity targeted for inhibition