Desiccation Dependent Structure and Stability of an Anhydrobiotic Nematode Late Embryogenesis Abundant (LEA) Protein

2009 ◽  
Author(s):  
Dai-xi Li ◽  
Xiaoming He
Keyword(s):  
Water Deficit ◽  
Structural Stability ◽  
Stress Proteins ◽  
Late Embryogenesis Abundant ◽  
Lea Proteins ◽  
Lea Protein ◽  
Late Embryogenesis ◽  
Severe Water Deficit ◽  
Space Filler ◽  
Group 3

A number of organisms have been found to be capable of surviving severe water deficit as a result of extreme drought and cold in nature by entering a state of suspended animation (i.e., anhydrobiosis or life without water) [1]. Although the precise molecular repertoire of desiccation tolerance in anhydrobiotic organisms is still not fully understood, results from recent studies indicate the crucial role of stress proteins such as the late embryogenesis abundant (LEA) proteins [2]. LEA proteins have been proposed to play a variety of roles in protecting biologicals from damaging by dehydration stress such as molecular chaperone and shield, ion chelator, antioxidant, and space filler. The multifunctional capacity of LEA proteins has been attributed in part to their structural plasticity: they are unfolded and when fully hydrated and become folded during water deficit [1]. However, the structural stability of LEA protein in response to desiccation is still not fully understood. In this study, the structure alteration of a group 3 LEA protein from an anhydrobiotic nematode (AavLEA1) [2] were investigated using the molecular dynamics (MD) simulation approach to understand the structural stability at different water contents.

scholarly journals Overexpression of ZmDHN11 could enhance transgenic yeast and tobacco tolerance to osmotic stress

2021 ◽  
Author(s):  
huining Ju ◽  
daxing Li ◽  
Dequan Li ◽  
Xinghong Yang ◽  
Yang Liu
Keyword(s):  
Osmotic Stress ◽  
Stress Proteins ◽  
Plant Stress ◽  
Late Embryogenesis Abundant ◽  
Water Deficit Stress ◽  
Lea Proteins ◽  
Lea Protein ◽  
Transgenic Yeast ◽  
Late Embryogenesis ◽  
Group Ii

Abstract Late embryogenesis abundant (LEA) proteins are widely assumed to play crucial roles in environmental stress tolerance, but their function has remained obscure. Dehydrins are group II LEA proteins, which are highly hydrophilic plant stress proteins. In the present study, a novel group II LEA protein, ZmDHN11 was cloned and identified from maize. The expression of ZmDHN11 was induced by high osmotic stress, low temperature, salinity and ABA (abscisic acid). The ZmDHN11 protein specifically accumulated in the nuclei and cytosol. Further study indicated that ZmDHN11 is phosphorylated by the casein kinase CKII. ZmDHN11 protected the activity of LDH under water deficit stress. The overexpression of ZmDHN11 endows transgenic yeast and tobacco with tolerance to osmotic stress.

scholarly journals KvLEA, a New Isolated Late Embryogenesis Abundant Protein Gene fromKosteletzkya virginicaResponding to Multiabiotic Stresses

2016 ◽  
Vol 2016 ◽  
pp. 1-10 ◽  
Author(s):  
Xiaoli Tang ◽  
Hongyan Wang ◽  
Liye Chu ◽  
Hongbo Shao
Keyword(s):  
Abiotic Stresses ◽  
Stress Proteins ◽  
Bioinformatic Analysis ◽  
Late Embryogenesis Abundant ◽  
Late Embryogenesis Abundant Protein ◽  
Lea Proteins ◽  
Lea Gene ◽  
Late Embryogenesis ◽  
Kosteletzkya Virginica ◽  
Multiple Sequences

The LEA proteins are a kind of hydrophilic proteins, playing main functions in desiccation tolerance. However, their importance as a kind of stress proteins in abiotic stress is being clarified little by little. In this study we isolated, cloned, and identified the firstKvLEAgene inKosteletzkya virginica. Bioinformatic analysis showed that the protein encoded by this gene had common properties of LEA proteins and the multiple sequences alignment and phylogenetic analysis further showed that this protein had high homology with twoArabidopsisLEA proteins. Gene expression analysis revealed that this gene had a higher expression in root and it was induced obviously by salt stress. Moreover, the transcripts ofKvLEAwere also induced by other abiotic stresses including drought, high temperature, chilling, and ABA treatment. Among these abiotic stresses, ABA treatment brought about the biggest changes to this gene. Collectively, our research discovered a novel LEA gene and uncovered its involvement in multiabiotic stresses inK. virginica. This research not only enriched studies on LEA gene in plant but also would accelerate more studies onK. virginicain the future.

Characterization of a group 1 late embryogenesis abundant protein in encysted embryos of the brine shrimp Artemia franciscana

2009 ◽  
Vol 87 (2) ◽  
pp. 415-430 ◽  
Author(s):  
Michelle A. Sharon ◽  
Anna Kozarova ◽  
James S. Clegg ◽  
Panayiotis O. Vacratsis ◽  
Alden H. Warner
Keyword(s):  
Amino Acids ◽  
Brine Shrimp ◽  
Animal Species ◽  
Late Embryogenesis Abundant ◽  
Lea Proteins ◽  
Lea Protein ◽  
Late Embryogenesis ◽  
Its Gene ◽  
Group 1

Late embryogenesis abundant (LEA) proteins are hydrophilic molecules that are believed to function in desiccation and low-temperature tolerance in some plants and plant propagules, certain prokaryotes, and several animal species. The brine shrimp Artemia franciscana can produce encysted embryos (cysts) that enter diapause and are resistant to severe desiccation. This ability is based on biochemical adaptations, one of which appears to be the accumulation of the LEA protein that is the focus of this study. The studies described herein characterize a 21 kDa protein in encysted Artemia embryos as a group 1 LEA protein. The amino acid sequence of this protein and its gene have been determined and entered into the NCBI database (no. EF656614). The LEA protein consists of 182 amino acids and it is extremely hydrophilic, with glycine (23%), glutamine (17%), and glutamic acid (12.6%) being the most abundant amino acids. This protein also consists of 8 tandem repeats of a 20 amino acid sequence, which is characteristic of group 1 LEA proteins from non-animal species. The LEA protein and its gene are expressed only in encysted embryos and not in larvae or adults. Evidence is presented to show that the LEA protein functions in the prevention of drying-induced protein aggregation, which supports its functional role in desiccation tolerance. This report describes, for the first time, the purification and characterization of a group 1 LEA protein from an animal species.

scholarly journals Late Embryogenesis Abundant (LEA) proteins confer water stress tolerance to mammalian somatic cells

2019 ◽  
Author(s):  
M Czernik ◽  
A Fidanza ◽  
FP Luongo ◽  
L Valbonetti ◽  
PA Scapolo ◽  
...  
Keyword(s):  
Protective Action ◽  
Somatic Cells ◽  
Late Embryogenesis Abundant ◽  
Lea Proteins ◽  
Water Stress Tolerance ◽  
Late Embryogenesis ◽  
Protein Group ◽  
Group 3 ◽  
Rehydration Process ◽  
Very High

AbstractLate Embryogenesis Abundant (LEA) proteins are commonly found in organisms capable of undergoing reversible dehydration - “anhydrobiosis”. Here, we have produced three LEA proteins: pTag-RAB17-GFP-N, Zea mays dehydrin-1dhn, expressed in the nucleo-cytoplasm; pTag-WCOR410-RFP, Tricum aestivum cold acclimation protein WCOR410, binding to cellular membranes, and pTag-LEA-BFP, Artemia franciscana LEA protein group 3 that targets the mitochondria. Somatic cells transfected with three LEA proteins were subjected to desiccation under controlled conditions, followed by rehydration, viability assessment and membrane/mitochondria functional tests were performed. Results shown that LEA protect cells from desiccation injury. Cells expressed all LEA proteins shown very high percentage of viable cells (58%) after four hour of desiccation compare to un-transfected cells (1% cell alive). Plasmalemma, cytoskeleton and mitochondria appeared unaffected in LEA-expressing cells, confirming their protective action during the entire desiccation and rehydration process. Here, we show that natural xeroprotectants (LEA proteins) transiently expressed in somatic cells confer them desiccation tolerance.

scholarly journals Lea protein expression during cold-induced dehydration in the Arctic collembola Megaphorura arctica

2011 ◽  
Vol 63 (3) ◽  
pp. 681-683 ◽  
Author(s):  
Z.D. Popovic ◽  
Jelena Purac ◽  
Danijela Kojic ◽  
Elvira Pamer ◽  
M.R. Worland ◽  
...  
Keyword(s):  
Late Embryogenesis Abundant ◽  
The Arctic ◽  
Lea Proteins ◽  
Lea Protein ◽  
Cellular Processes ◽  
Cryoprotective Dehydration ◽  
Late Embryogenesis ◽  
Winter Temperatures ◽  
Number Of Genes ◽  
The Difference

The Arctic springtail Megaphorura arctica (Tullberg, 1876) employs a strategy known as cryoprotective dehydration to survive winter temperatures as low as -25?C. During cryoprotective dehydration, water is lost from the animal to ice in its surroundings as a result of the difference in vapour pressure between the animal?s supercooled body fluids and ice (Worland et al., 1998; Holmstrup and Somme, 1998). This mechanism ensures that as the habitat temperature falls, the concentration of solutes remains high enough to prevent freezing (Holmstrup et al., 2002). In M. arctica, accumulation of trehalose, a cryo/anhydro protectant, occurs in parallel with dehydration. Recent studies have identified a number of genes and cellular processes involved in cryoprotective dehydration in M. arctica (Clark et al., 2007; Clark et al., 2009; Purac et al., 2011). One of them includes late embryogenesis abundant (LEA) proteins. This study, together with that of Bahrndorff et al. (2008), suggests that LEA proteins may be involved in protective dehydration in this species.

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