Abstract
In Arabidopsis thaliana, LONG-CHAIN ACYL-COA SYNTHETASEs (LACSs) catalyze the synthesis of long-chain acyl-CoAs and function in diverse biological processes. We have recently revealed that LACS2 is primarily involved in the production of polyunsaturated linolenoyl-CoA, essential for the activation of ethylene response transcription factors-mediated hypoxia signaling. Here, we further reported the dual role of LACS2 in the regulation of submergence tolerance by modulating cuticle permeability in Arabidopsis cells. LACS2-overexpressors (LACS2-OEs) showed improved tolerance to submergence, with higher accumulation of cuticular wax and cutin in their rosettes. In contrast, knockout of LACS2 in the lacs2-3 mutant resulted in hypersensitivity to submergence with reduced wax crystals and thinner cutin layer. By analyses of plant surface permeability, we observed that the hypoxic sensitivities in the LACS2-OEs and lacs2-3 mutant were physiologically correlated with chlorophyll leaching, water loss rates, ionic leakage, and gas exchange. Thus, our findings suggest the role of LACS2 in plant response to submergence by modulating cuticle permeability in plant cells.
Highlights
Submergence-induced hypoxia is one of the most important abiotic stresses, which seriously affects plant growth, development, and yields [1]
We have previously demonstrated that Arabidopsis LACS2 plays an essential role in hypoxia
We have previously demonstrated that Arabidopsis LACS2 plays an essential role in hypoxia signaling by modulating long-chain acyl-CoA pools and ERF-VII–ACBP dynamics [8]
Summary
Submergence-induced hypoxia is one of the most important abiotic stresses, which seriously affects plant growth, development, and yields [1]. To cope with the insufficient oxygen supply under long-term submergence conditions, plants have developed a series of adaptations at cellular, tissue, and organismal levels [1]. These processes are tightly under the regulation of multiple signaling networks and their interaction [2,3,4,5]. RAP2.12 is released from the ACBP1–ERF-VII complex and translocated into the nucleus to activate the expression of hypoxia-responsive genes. Upon reoxygenation, the levels of ERF-VII proteins are controlled by ubiquitination and degradation though the N-end rule proteolysis pathway [1,4]. Two independent studies reveal that under hypoxia, lipid signals promote the dissociation of RAP2.12
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