Abstract
Legumes play an important role in ensuring food security, improving nutrition and enhancing ecosystem resilience. Chickpea is a globally important grain legume adapted to semi-arid regions under rain-fed conditions. A growing body of research shows that aldehyde dehydrogenases (ALDHs) represent a gene class with promising potential for plant adaptation improvement. Aldehyde dehydrogenases constitute a superfamily of proteins with important functions as ‘aldehyde scavengers’ by detoxifying aldehydes molecules, and thus play important roles in stress responses. We performed a comprehensive study of the ALDH superfamily in the chickpea genome and identified 27 unique ALDH loci. Most chickpea ALDHs originated from duplication events and the ALDH3 gene family was noticeably expanded. Based on the physical locations of genes and sequence similarities, our results suggest that segmental duplication is a major driving force in the expansion of the ALDH family. Supported by expression data, the findings of this study offer new potential target genes for improving stress tolerance in chickpea that will be useful for breeding programs.
Highlights
Aldehyde molecules are common intermediates of a number of catabolic and biosynthetic pathways that are produced in response to biotic and abiotic environmental stresses
As exhibited in other plant species, the wide range of pIs suggests that the chickpea aldehyde dehydrogenases (ALDHs) proteins can work in various different subcellular environments, which is in accordance with the subcellular localization predicted for the sequences revealing that 44.4% (12 out 27) of C. arietinum non-redundant ALDH genes (CaALDH) can be localized to the cytoplasm (Table S1)
The classification of protein families was made according to the criteria established by the ALDH Gene Nomenclature Committee (AGNC), namely the protein root symbol (ALDH) was followed by a family description number (1, 2, 3, etc.), a subfamily descriptor (A, B, C, etc.) and an individual gene number
Summary
Aldehyde molecules are common intermediates of a number of catabolic and biosynthetic pathways that are produced in response to biotic and abiotic environmental stresses. The aldehyde dehydrogenase (ALDH) superfamily is a group of NAD(P)+-dependent enzymes that catalyze the irreversible oxidation of a wide range of reactive aldehydes to their corresponding carboxylic acids [3,4]. Under conditions inducing oxidative stress, ALDH enzymes act as ‘aldehyde scavengers’ by metabolizing reactive aldehydes derived as lipid peroxidation-derived aldehydes, which are potentially toxic due to their extreme reactivity with the nucleophilic compounds such as nucleic acids, proteins and membrane lipids [5,6]. ALDH activity may serve to fine-tune gene activation since ALDHs may modulate signaling by lipid peroxidation-derived bioactive aldehydes [7]. ALDHs have been identified and categorized into 24 separate families based on protein sequence identity as main criteria [9], and by their functionality [10,11]
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