LEA Protein Function in Plant Abiotic Stress Tolerance

Late embryogenesis abundant (LEA) proteins constitute a diverse family of highly hydrophilic and often intrinsically disordered polypeptides that accumulate in plant tissues during seed maturation and in vegetative organs exposed to dehydration, salinity, extreme temperatures or osmotic stress. Their unstructured nature under aqueous conditions enables LEA proteins to remain soluble at low water potential and to undergo conformational changes, adopting α-helical or coiled-coil motifs upon interaction with membranes, ions or other macromolecules. Through chaperone-like activity, LEA proteins stabilise membranes, protect enzyme structure and prevent aggregation of cellular constituents. Gene family expansion via segmental and whole-genome duplication, combined with diverse promoter architectures, has allowed specialised expression across developmental stages and stress environments. Collectively, these proteins underpin key adaptive mechanisms that maintain cellular homeostasis under abiotic stress, with broad implications for improving drought, salinity and cold tolerance in crops.

Research from Nature Portfolio

A comprehensive genome-wide survey in oilseed rape revealed 108 LEA genes classified into eight subfamilies based on conserved domains. Analyses demonstrated that segmental duplication and whole-genome duplication events drove family expansion, while synteny mapping highlighted high conservation across related species despite occasional gene gains and losses. Expression profiling showed that most LEA genes are upregulated in vegetative leaves and in late-stage seeds, suggesting dual roles in vegetative stress defence and seed desiccation tolerance. This work provides a foundational framework for targeted manipulation of LEA genes to enhance resilience in polyploid crops.

LEA Protein Function in Plant Abiotic Stress Tolerance publication trend

The graph below shows the total number of articles in lea protein function in plant abiotic stress tolerance across all publications each year (not limited to Nature Index journals).

Technical terms

Late embryogenesis abundant (LEA) proteins: A family of hydrophilic, often unstructured plant proteins that accumulate during seed desiccation and in vegetative tissues under abiotic stress.

Intrinsically disordered proteins (IDPs): Proteins lacking stable tertiary structure under physiological conditions, enabling flexibility and interaction with multiple partners.

Chaperone-like activity: The ability of a protein to prevent aggregation or denaturation of other proteins and stabilise cellular structures under stress.

Oligomerisation: Assembly of protein monomers into multi-subunit complexes, which can modulate functional properties such as molecular shielding or structural support.

Segmental duplication: A form of gene duplication in which chromosomal segments, including one or more genes, are duplicated within the genome, contributing to gene family expansion.

References

1. Functional in vitro diversity of an intrinsically disordered plant protein during freeze–thawing is encoded by its structural plasticity. Protein Science (2024).
2. Characterization of the late embryogenesis abundant (LEA) proteins family and their role in drought stress tolerance in upland cotton. BMC Genomic Data (2018).
3. Genome-wide identification, structural analysis and new insights into late embryogenesis abundant (LEA) gene family formation pattern in Brassica napus. Scientific Reports (2016).