LEA Proteins During Water Stress: Not Just for Plants Anymore

Abstract

Introduction

Improved tolerance to salt and water stress in Drosophila melanogaster cells conferred by late embryogenesis abundant protein

“…When water is removed, most LEA proteins assume their 'native' conformation, which often consists of a high percentage of α-helix (for reviews see (Hand et al, 2011;Tunnacliffe and Wise, 2007)). For example, molecular dynamics simulation of a LEA protein fragment from the nematode Aphelenchus avenae showed no substantial increase in α-helix during reductions in the protein water content from 80 to 30 wt%.…”

“…A recurring strategy in animals to tolerate extreme water loss is the expression of LEA proteins with or without the concurrent accumulation of large amounts of the non-reducing disaccharide trehalose (Goyal et al, 2005;Hand et al, 2011;Oliver et al, 2001;Tunnacliffe and Lapinski, 2003;Watanabe et al, 2005). LEA proteins were first described about 30 years ago in desiccation tolerant cotton seeds at maturation (Dure and Galau, 1981;Galau, 1986) and were thought to be unique to plants.…”

“…LEA proteins were found to reduce the damage to seeds and seedlings by harsh environmental conditions such as drought, freezing, and osmotic stress (Bray, 1993;Espelund et al, 1992;Hundertmark and Hincha, 2008;Pammenter and Berjak, 1999;Shih et al, 2008). Our knowledge about the occurrence of LEA and LEA-like proteins in animals is increasing rapidly, and since 2000, when the first LEA-like protein was reported in an invertebrate species (Solomon et al, 2000), more than 30 other LEA and LEA-like protein sequences have been deposited into the database of the National Center for Biotechnology Information (NCBI) from animals belonging to several phyla including Arthropoda, Rotifera, and Nematoda (Hand et al, 2011).…”

Disordered Cold Regulated15 Proteins Protect Chloroplast Membranes during Freezing through Binding and Folding, But Do Not Stabilize Chloroplast Enzymes in Vivo

“…These cold-induced transcription factors activate downstream target genes encoding enzymes involved in compatible solute biosynthesis and cold-regulated (COR) proteins, many of which belong to the group of late-embryogenesis abundant (LEA) proteins (Thomashow, 1999;Hundertmark and Hincha, 2008). LEA proteins have been found not only in plants but also in freezing and desiccation-tolerant invertebrates (Browne et al, 2002;Hand et al, 2011).…”

Late embryogenesis abundant proteins protect human hepatoma cells during acute desiccation

“…Many organisms accumulate compatible osmolytes of low molecular weight for osmotic balance during water stress (11,12), and some have solutes, such as trehalose, that can stabilize biological structures during desiccation (6,7,13). More recent investigations underscore the contributions of various protective proteins during drying, including stress proteins (14), late embryogenesis abundant (LEA) proteins, and anhydrin (15,16), the latter two being intrinsically disordered proteins (17,18). In the present study, we ectopically expressed two different LEA proteins in human hepatocellular carcinoma (HepG2) cells in the presence and absence of intracellular trehalose.…”