Abiotic and biotic stresses induce the formation of reactive oxygen species (ROS), which subsequently causes the excessive accumulation of aldehydes in cells. Stress-derived aldehydes are commonly designated as reactive electrophile species (RES) as a result of the presence of an electrophilic α, β-unsaturated carbonyl group. Aldehyde dehydrogenases (ALDHs) are NAD(P)+-dependent enzymes that metabolize a wide range of endogenous and exogenous aliphatic and aromatic aldehyde molecules by oxidizing them to their corresponding carboxylic acids. The ALDH enzymes are found in nearly all organisms, and plants contain fourteen ALDH protein families. In this review, we performed a critical analysis of the research reports over the last decade on plant ALDHs. Newly discovered roles for these enzymes in metabolism, signaling and development have been highlighted and discussed. We concluded with suggestions for future investigations to exploit the potential of these enzymes in biotechnology and to improve our current knowledge about these enzymes in gene signaling and plant development.
Plants are sessile in nature and they perceive and react to environmental stresses such as abiotic and biotic factors. These induce a change in the cellular homeostasis of reactive oxygen species (ROS). ROS are known to react with cellular components, including DNA, lipids, and proteins, and to interfere with hormone signaling via several post-translational modifications (PTMs). Protein carbonylation (PC) is a non-enzymatic and irreversible PTM induced by ROS. The non-enzymatic feature of the carbonylation reaction has slowed the efforts to identify functions regulated by PC in plants. Yet, in prokaryotic and animal cells, studies have shown the relevance of protein carbonylation as a signal transduction mechanism in physiological processes including hydrogen peroxide sensing, cell proliferation and survival, ferroptosis, and antioxidant response. In this review, we provide a detailed update on the most recent findings pertaining to the role of PC and its implications in various physiological processes in plants. By leveraging the progress made in bacteria and animals, we highlight the main challenges in studying the impacts of carbonylation on protein functions in vivo and the knowledge gap in plants. Inspired by the success stories in animal sciences, we then suggest a few approaches that could be undertaken to overcome these challenges in plant research. Overall, this review describes the state of protein carbonylation research in plants and proposes new research avenues on the link between protein carbonylation and plant redox biology.
Protein carbonylation is a post‐translational modification associated with the reactive oxygen species. It results from the direct oxidation of the side chains of Lys, Arg, Pro, and Thr residues by hydroxyl radical HO• or the addition of reactive carbonyl species including α,β‐unsaturated aldehydes and oxylipins to the side chain of Cys, His, and Lys. Recent findings indicated that the phytohormone abscisic acid (ABA) induces the production of α,β‐unsaturated aldehydes that modulate the effect of ABA on stomatal closure. This indicated that α,β‐unsaturated aldehydes might mediate ABA signaling. In this study, we investigated the ABA‐induced protein carbonylation events by profiling the carbonylated proteome extracted from Arabidopsis thaliana leaves after ABA treatment. The carbonylated proteins were enriched by affinity chromatography and subjected to liquid chromatography–tandem mass spectrometry. We identified 180 carbonylated proteins. Of these, 26 proteins became carbonylated upon ABA treatment, whereas 163 proteins that were carbonylated in untreated samples were no longer detected in the ABA‐treated samples, which points to dynamic control of protein carbonylation by ABA in A. thaliana. A few regulatory stress‐related proteins and enzymes involved in the biosynthesis of the aspartate family of amino acids were overrepresented in the list of proteins, which the carbonylation status changed between untreated and ABA‐treated samples. These results indicated that ABA triggers a change in the pattern of protein carbonylation in A. thaliana. This change is independent of the commonly seen increased levels of carbonylated proteins in the plants subjected to deadly stress conditions.
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