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Late embryogenesis abundant (LEA) proteins play a crucial role in the desiccation tolerance of resurrection plants, although their exact functions remain unclear. Therefore, we recombinantly produced desiccation-induced LEA4 protein member, RsLEAP30-His6, from Ramonda serbica and investigated its structural behaviour under simulated dehydration conditions. This is the first report on the production and purification of a recombinant LEA protein from the resurrection plant R. serbica . By immobilised metal affinity and size-exclusion chromatography, we successfully obtained RsLEAP30-His6 with a purity of over 95%, thus providing a robust and scalable method that can also be used for the production of other LEA proteins. Structural characterisation by circular dichroism spectroscopy in combination with in silico modelling, revealed that RsLEAP30 is predominantly disordered under fully hydrated conditions, whereas it adopts an α-helical structure under desiccation-like conditions and in the presence of a lipid mimetic. This disorder-to-order transition underpins the possible protective role of RsLEAP30 in chloroplasts, likely through interactions with thylakoids and desiccation-sensitive proteins enabling the rapid recovery of photosynthetic components upon rehydration. Our study provides new insights into the structure–function relationship of LEA proteins in desiccation tolerance and creates a basis for future bioengineering strategies to improve crop drought tolerance.

Plants are exposed to different external conditions that affect growth, development, and productivity. Water deficit is one of these adverse conditions caused by drought, salinity, and extreme temperatures. Plants have developed different responses to prevent, ameliorate or repair the damage inflicted by these stressful environments. One of these responses is the activation of a set of genes encoding a group of hydrophilic proteins that typically accumulate to high levels during seed dehydration, at the last stage of embryogenesis, hence named Late Embryogenesis Abundant (LEA) proteins. LEA proteins also accumulate in response to water limitation in vegetative tissues, and have been classified in seven groups based on their amino acid sequence similarity and on the presence of distinctive conserved motifs. These proteins are widely distributed in the plant kingdom, from ferns to angiosperms, suggesting a relevant role in the plant response to this unfavorable environmental condition. In this review, we analyzed the LEA proteins from those legumes whose complete genomes have been sequenced such as Phaseolus vulgaris, Glycine max, Medicago truncatula, Lotus japonicus, Cajanus cajan, and Cicer arietinum. Considering their distinctive motifs, LEA proteins from the different groups were identified, and their sequence analysis allowed the recognition of novel legume specific motifs. Moreover, we compile their transcript accumulation patterns based on publicly available data. In spite of the limited information on these proteins in legumes, the analysis and data compiled here confirm the high correlation between their accumulation and water deficit, reinforcing their functional relevance under this detrimental conditions.

Key message MfLEA3 is involved in protection of catalase activity and confers multiple abiotic stress tolerance. Late embryogenesis abundant (LEA) proteins are involved in plant growth, development and abiotic stress tolerance. A member of group 3 LEA proteins from Medicago sativa subsp. falcata (L.) Arcang, MfLEA3, was investigated in the study. MfLEA3 transcript was induced in response to cold, dehydration, and abscisic acid (ABA), while the cold-induced transcript of MfLEA3 was blocked by pretreatment with inhibitor of ABA synthesis. Constitutive expression of MfLEA3 led to enhanced tolerance to cold, drought, and high-light stress in transgenic tobacco plants. Compared to accumulated reactive oxygen species (ROS) in the wild-type in response to treatments with low temperature, drought, and high light, ROS were not accumulated in transgenic plants. Superoxide dismutase, catalase (CAT), and ascorbate-peroxidase activities were increased in all plants after treatments with the above stresses, while higher CAT activity was maintained in transgenic plants compared with wild-type. However, transcript level of CAT-encoding genes including CAT1 , CAT2, and CAT3 showed no significant difference between transgenic plants and wild-type, indicating that the higher CAT activity was not associated with its gene expression. ABA sensitivity and transcripts of several ABA and stress-responsive genes showed no difference between transgenic plant and wild-type, indicating that ABA signaling was not affected by constitutive expression of MfLEA3 . The results suggest that MfLEA3 may be involved in the protection of CAT activity and confers multiple abiotic stress tolerance.

Late embryogenesis abundant (LEA) proteins are part of a large protein family that protect other proteins from aggregation due to desiccation or osmotic stresses. Recently, the seed proteome was characterized by 2D-PAGE and one highly accumulated protein spot was identified as a LEA protein and was named AcLEA. In this work, cDNA was cloned into an expression vector and the recombinant protein was purified and characterized. encodes a 172 amino acid polypeptide with a predicted molecular mass of 18.34 kDa and estimated p of 8.58. Phylogenetic analysis revealed that AcLEA is evolutionarily close to the LEA3 group. Structural characteristics were revealed by nuclear magnetic resonance and circular dichroism methods. We have shown that recombinant AcLEA is an intrinsically disordered protein in solution even at high salinity and osmotic pressures, but it has a strong tendency to take a secondary structure, mainly folded as α-helix, when an inductive additive is present. Recombinant AcLEA function was evaluated using as model showing the important protection role against desiccation, oxidant conditions, and osmotic stress. AcLEA recombinant protein was localized in cytoplasm of protoplasts and orthologs were detected in seeds of wild and domesticated amaranth species. Interestingly AcLEA was detected in leaves, stems, and roots but only in plants subjected to salt stress. This fact could indicate the important role of AcLEA protection during plant stress in all amaranth species studied.

Cells of many organisms and organs can withstand an (almost) total water loss (anhydrobiosis). Sugars play an essential role in desiccation tolerance due to their glass formation ability during dehydration. In addition, intrinsically disordered LEA proteins contribute to cellular survival under such conditions. One possible mechanism of LEA protein function is the stabilization of sugar glasses. However, little is known about the underlying mechanisms. Here we used FTIR spectroscopy to investigate sucrose (Suc) glass stability dried from water or from two buffer components in the presence of four recombinant LEA and globular reference proteins. Buffer ions influenced the strength of the Suc glass in the order Suc < Suc/Tris < Suc/NaP. LEA proteins strengthened the sugar H-bonded network and the molecular structure in the glassy state. The position of νOH peak and the wavenumber–temperature coefficient (WTCg) provided similar information about the H-bonded network. Protein aggregation of LEA proteins was reduced in the desiccation-induced Suc glassy state. Detailed knowledge about the role of LEA proteins in the stabilization of dry sugar glasses yields information about their role in anhydrobiosis. This may open the possibility to use such proteins in biotechnical applications requiring dry storage of biologicals such as proteins, cells or tissues.

Challenging environmental conditions are major factors that severely affect plant growth and limit agricultural productivity. To mitigate these stresses, plants have evolved various adaptive mechanisms. Among these, Late Embryogenesis Abundant (LEA) proteins play a pivotal role in responding to abiotic stresses and participate in a reciprocal regulatory network with the abscisic acid (ABA) signaling pathway. However, the precise molecular mechanisms underlying this reciprocity and the full composition of this network require systematic integration. This review synthesizes recent advances to propose a novel \"ABA-LEA feedback loop\" model and presents a comprehensive analysis of the classification into seven groups, structural features, molecular functions and mechanisms by which LEA proteins contribute to plant stress resistance. Special emphasis is placed on the intricate interplay between LEA proteins and the ABA signaling pathway, encompassing both the ABA-dependent regulation of expression and the reciprocal feedback exerted by LEA proteins on ABA signaling through mechanisms that influence ABA homeostasis and signaling. By synthesizing evidence for this reciprocal regulation, this review establishes a novel feedback loop model that redefines LEA proteins as active modulators rather than passive effectors in stress signaling, offering new theoretical targets for breeding stress-resilient crops.

Late Embryogenesis Abundant (LEA) proteins play vital roles in plant responses to abiotic stress and developmental regulation. Pineapple (Ananas comosus L.) is a major tropical fruit crop with high economic value, but its production is often threatened by cold stress, particularly in regions at the northern margin of its cultivation. Despite the recognized importance of LEA proteins in stress adaptation, their genomic landscape and functional characteristics in pineapple remain largely unexplored. In this study, 37 AcLEA genes were identified in the pineapple (Ananas comosus L.) genome and classified into six subfamilies, with LEA_2 being the largest. Most AcLEA proteins were predicted to be hydrophilic, thermally stable, and intrinsically disordered, consistent with typical LEA protein characteristics. Phylogenetic and collinearity analyses revealed species-specific expansion patterns, primarily driven by segmental duplication events. Most duplicated gene pairs shared similar exon–intron structures, motif compositions, and expression profiles, although several displayed signs of functional divergence based on distinct expression patterns, Ka/Ks ratios > 1, and motif differences. Promoter cis-element, transcription factor, and miRNA network predictions indicated that AcLEA genes are widely involved in stress responses as well as growth and development. Expression profiling showed that many AcLEA genes including AcLEA32, AcLEA7, AcLEA9, AcLEA30, AcLEA29, AcLEA33, and AcLEA18 were significantly upregulated under cold stress and declined upon stress removal, indicating a potential role in cold tolerance. Some AcLEA genes, such as AcLEA32 and AcLEA33, showed faster and stronger induction under cold stress in the cold-tolerant cultivar “Comte de Paris” (BL) compared to the sensitive cultivar “Tainong No. 20” (NN), suggesting that differential gene responsiveness may contribute to cultivar-specific cold tolerance. Additionally, most AcLEA genes exhibited distinct spatiotemporal expression patterns across floral organs and fruit at various developmental stages, suggesting their involvement in reproductive development. These findings provide a foundation for future functional studies and highlight candidate genes for improving cold resilience and developmental traits in pineapple through molecular breeding.

Late embryogenesis abundant (LEA) proteins constitute a large protein family that is closely associated with resistance to abiotic stresses in multiple organisms and protect cells against drought and other stresses. Azotobacter vinelandii is a soil bacterium that forms desiccation-resistant cysts. This bacterium possesses two genes, here named lea1 and lea2, coding for avLEA1 and avLEA2 proteins, both containing 20-mer motifs characteristic of eukaryotic plant LEA proteins. In this study, we found that disruption of the lea1 gene caused a loss of the cysts' viability after 3 months of desiccation, whereas at 6 months, wild-type or lea2 mutant strain cysts remained viable. Vegetative cells of the lea1 mutant were more sensitive to osmotic stress; cysts developed by this mutant were also more sensitive to high temperatures than cysts or vegetative cells of the wild type or of the lea2 mutant. Expression of lea1 was induced several fold during encystment. In addition, the protective effects of these proteins were assessed in Escherichia coli cells. We found that E. coli cells overexpressing avLEA1 were more tolerant to salt stress than control cells; finally, in vitro analysis showed that avLEA1 protein was able to prevent the freeze thaw-induced inactivation of lactate dehydrogenase. In conclusion, avLEA1 is essential for the survival of A. vinelandii in dry conditions and for protection against hyper-osmolarity, two major stress factors that bacteria must cope with for survival in the environment. This is the first report on the role of bacterial LEA proteins on the resistance of cysts to desiccation.

ABA is a major plant hormone that plays important roles during many phases of plant life cycle, including seed development, maturity and dormancy, and especially the acquisition of desiccation tolerance. Understanding of the molecular basis of ABA-mediated plant response to stress is of interest not only in basic research on plant adaptation but also in applied research on plant productivity. Maize mutant viviparous-5 (vp5), deficient in ABA biosynthesis in seeds, is a useful material for studying ABA-mediated response in maize. Due to carotenoid deficiency, vp5 endosperm is white, compared to yellow Vp5 endosperm. However, the background difference at proteome level between vp5 and Vp5 seeds is unclear. This study aimed to characterize proteome alterations of maize vp5 seeds and to identify ABA-dependent proteins during seed maturation. We compared the embryo and endosperm proteomes of vp5 and Vp5 seeds by gel-based proteomics. Up to 46 protein spots, most in embryos, were found to be differentially accumulated between vp5 and Vp5. The identified proteins included small heat shock proteins (sHSPs), late embryogenesis abundant (LEA) proteins, stress proteins, storage proteins and enzymes among others. However, EMB564, the most abundant LEA protein in maize embryo, accumulated in comparable levels between vp5 and Vp5 embryos, which contrasted to previously characterized, greatly lowered expression of emb564 mRNA in vp5 embryos. Moreover, LEA proteins and sHSPs displayed differential accumulations in vp5 embryos: six out of eight identified LEA proteins decreased while nine sHSPs increased in abundance. Finally, we discussed the possible causes of global proteome alterations, especially the observed differential accumulation of identified LEA proteins and sHSPs in vp5 embryos. The data derived from this study provides new insight into ABA-dependent proteins and ABA-mediated response during maize seed maturation.

Salinity stress is considered the most devastating abiotic stress for crop productivity. Accumulating different types of soluble proteins has evolved as a vital strategy that plays a central regulatory role in the growth and development of plants subjected to salt stress. In the last two decades, efforts have been undertaken to critically examine the genome structure and functions of the transcriptome in plants subjected to salinity stress. Although genomics and transcriptomics studies indicate physiological and biochemical alterations in plants, it do not reflect changes in the amount and type of proteins corresponding to gene expression at the transcriptome level. In addition, proteins are a more reliable determinant of salt tolerance than simple gene expression as they play major roles in shaping physiological traits in salt-tolerant phenotypes. However, little information is available on salt stress-responsive proteins and their possible modes of action in conferring salinity stress tolerance. In addition, a complete proteome profile under normal or stress conditions has not been established yet for any model plant species. Similarly, a complete set of low abundant and key stress regulatory proteins in plants has not been identified. Furthermore, insufficient information on post-translational modifications in salt stress regulatory proteins is available. Therefore, in recent past, studies focused on exploring changes in protein expression under salt stress, which will complement genomic, transcriptomic, and physiological studies in understanding mechanism of salt tolerance in plants. This review focused on recent studies on proteome profiling in plants subjected to salinity stress, and provide synthesis of updated literature about how salinity regulates various salt stress proteins involved in the plant salt tolerance mechanism. This review also highlights the recent reports on regulation of salt stress proteins using transgenic approaches with enhanced salt stress tolerance in crops.