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S‐nitrosylated proteins of a medicinal CAM plant Kalanchoe pinnata – ribulose‐1,5‐bisphosphate carboxylase/oxygenase activity targeted for inhibition
Author(s) -
Abat Jasmeet K.,
Mattoo Autar K.,
Deswal Renu
Publication year - 2008
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2008.06425.x
Subject(s) - rubisco , biochemistry , oxygenase , crassulacean acid metabolism , s nitrosylation , arabidopsis thaliana , ribulose 1,5 bisphosphate , pyruvate carboxylase , biology , chemistry , photosynthesis , enzyme , cysteine , gene , mutant
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 NaH 14 CO 3 . The NO‐releasing compound S ‐nitrosoglutathione inhibited its activity in a dose‐dependent manner suggesting Rubisco inactivation by nitrosylation for the first time.