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

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.

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

ASME 2009 Summer Bioengineering Conference, Parts A and B ◽

10.1115/sbc2009-206862 ◽

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.

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Intrinsically disordered chaperones in plants and animalsThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

Biochemistry and Cell Biology ◽

10.1139/o09-163 ◽

2010 ◽

Vol 88 (2) ◽

pp. 167-174 ◽

Cited By ~ 90

Author(s):

Peter Tompa ◽

Denes Kovacs

Keyword(s):

Stress Proteins ◽

Intrinsically Disordered Proteins ◽

Peer Review Process ◽

Plant Stress ◽

Late Embryogenesis Abundant ◽

Disordered Proteins ◽

Lea Proteins ◽

Intrinsically Disordered ◽

And Function

Intrinsically disordered proteins (IDPs) are widespread in eukaryotes and fulfill important functions associated with signaling and regulation. Recent evidence points to a special and thus largely disrespected functional capacity of IDPs—that they can assist the folding of other proteins and prevent their aggregation, i.e., that they can act as chaperones. In this paper, we survey current information available on this phenomenon, with particular focus on (i) the structure and function of IDPs in general, (ii) disordered chaperones in plants, (iii) disordered chaperones in other organisms spanning from insects to mammals, (iv) the possible mechanisms of action of disordered chaperones, and (v) the possibility of two-faced (Janus) chaperone activity of disordered chaperones, which can assist the folding of both RNA and protein substrates. The evidence is most conclusive in the case of plant stress proteins, such as late embryogenesis abundant (LEA) proteins or dehydrins. We will show that the cellular function of LEA proteins in mitigating the damage caused by stress is clear; nevertheless, experiments carried out in vivo must be extended and the molecular mechanism of the action of IDP chaperones also requires clarification. Using these details, we chart out how far the field has progressed only to emphasize the long road ahead before chaperone function can be firmly established as part of the physiological mechanistic arsenal of the emerging group of IDPs.

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

BioMed Research International ◽

10.1155/2016/9823697 ◽

2016 ◽

Vol 2016 ◽

pp. 1-10 ◽

Cited By ~ 4

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.

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

Biochemistry and Cell Biology ◽

10.1139/o09-001 ◽

2009 ◽

Vol 87 (2) ◽

pp. 415-430 ◽

Cited By ~ 43

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.

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Group II late embryogenesis abundant (LEA) proteins: structural and functional aspects in plant abiotic stress

Plant Growth Regulation ◽

10.1007/s10725-015-0113-3 ◽

2015 ◽

Vol 79 (1) ◽

pp. 1-17 ◽

Cited By ~ 84

Author(s):

Aditya Banerjee ◽

Aryadeep Roychoudhury

Keyword(s):

Abiotic Stress ◽

Late Embryogenesis Abundant ◽

Lea Proteins ◽

Functional Aspects ◽

Late Embryogenesis ◽

Group Ii ◽

Plant Abiotic Stress

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

Archives of Biological Sciences ◽

10.2298/abs1103681p ◽

2011 ◽

Vol 63 (3) ◽

pp. 681-683 ◽

Cited By ~ 3

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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