Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses

• Published in: Biomolecules (Basel, Switzerland) Switzerland), 2021-11, Vol.11 (11), p.1662
• Main Authors: Abdul Aziz, Mughair, Sabeem, Miloofer, Mullath, Sangeeta Kutty, Brini, Faical, Masmoudi, Khaled
• Format: Article
• Language: English
• Subjects: Abiotic stress; Abscisic acid; Cell division; Cold; Crystallization; Dehydration; dehydrins; Developmental stages; Drought; Embryogenesis; Embryos; Flowers & plants; gene expression; Gene Expression Regulation, Plant; Genes; Genome-wide association studies; Genome-Wide Association Study; Genomics; group II LEA protein; hydrophilins; Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - genetics; Intrinsically Disordered Proteins - metabolism; Low temperature; Plant cells; Plant protection; Plant Proteins - chemistry; Plant Proteins - genetics; Plant Proteins - metabolism; Plants - genetics; Plants - metabolism; Proteins; Review; Salinity; Seeds; Seeds - genetics; Seeds - metabolism; Signal transduction; Stress, Physiological
• ISSN: 2218-273X; 2218-273X
• DOI: 10.3390/biom11111662

In response to various environmental stresses, plants have evolved a wide range of defense mechanisms, resulting in the overexpression of a series of stress-responsive genes. Among them, there is certain set of genes that encode for intrinsically disordered proteins (IDPs) that repair and protect the plants from damage caused by environmental stresses. Group II LEA (late embryogenesis abundant) proteins compose the most abundant and characterized group of IDPs; they accumulate in the late stages of seed development and are expressed in response to dehydration, salinity, low temperature, or abscisic acid (ABA) treatment. The physiological and biochemical characterization of group II LEA proteins has been carried out in a number of investigations because of their vital roles in protecting the integrity of biomolecules by preventing the crystallization of cellular components prior to multiple stresses. This review describes the distribution, structural architecture, and genomic diversification of group II LEA proteins, with some recent investigations on their regulation and molecular expression under various abiotic stresses. Novel aspects of group II LEA proteins in and in orthodox seeds are also presented. Genome-wide association studies (GWAS) indicated a ubiquitous distribution and expression of group II LEA genes in different plant cells. In vitro experimental evidence from biochemical assays has suggested that group II LEA proteins perform heterogenous functions in response to extreme stresses. Various investigations have indicated the participation of group II LEA proteins in the plant stress tolerance mechanism, spotlighting the molecular aspects of group II LEA genes and their potential role in biotechnological strategies to increase plants' survival in adverse environments.