scholarly journals Characterization of the Heat-Stable Proteome During Seed Germination in Arabidopsis with Special Focus on LEA Proteins

2021 ◽  
Vol 22 (15) ◽  
pp. 8172
Author(s):  
Orarat Ginsawaeng ◽  
Michal Gorka ◽  
Alexander Erban ◽  
Carolin Heise ◽  
Franziska Brueckner ◽  
...  
Keyword(s):  
Seed Germination ◽  
Seedling Establishment ◽  
Intrinsically Disordered Proteins ◽  
Late Embryogenesis Abundant ◽  
Disordered Proteins ◽  
Similar Proportion ◽  
Special Focus ◽  
Lea Proteins ◽  
Intrinsically Disordered ◽  
Heat Stable

During seed germination, desiccation tolerance is lost in the radicle with progressing radicle protrusion and seedling establishment. This process is accompanied by comprehensive changes in the metabolome and proteome. Germination of Arabidopsis seeds was investigated over 72 h with special focus on the heat-stable proteome including late embryogenesis abundant (LEA) proteins together with changes in primary metabolites. Six metabolites in dry seeds known to be important for seed longevity decreased during germination and seedling establishment, while all other metabolites increased simultaneously with activation of growth and development. Thermo-stable proteins were associated with a multitude of biological processes. In the heat-stable proteome, a relatively similar proportion of fully ordered and fully intrinsically disordered proteins (IDP) was discovered. Highly disordered proteins were found to be associated with functional categories development, protein, RNA and stress. As expected, the majority of LEA proteins decreased during germination and seedling establishment. However, four germination-specific dehydrins were identified, not present in dry seeds. A network analysis of proteins, metabolites and amino acids generated during the course of germination revealed a highly connected LEA protein network.

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.

2010 ◽  
Vol 88 (2) ◽  
pp. 167-174 ◽  
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.

scholarly journals Heat Stability of Proteins and Its Exploitation for Purification of Heat-Stable Proteins

2020 ◽  
Author(s):  
Muhammad Ahmad ◽  
Aisha Tahir ◽  
Rana Salman Anjum
Keyword(s):  
Heat Treatment ◽  
Intrinsically Disordered Proteins ◽  
Three Dimensional ◽  
Heat Stability ◽  
Treatment Method ◽  
Disordered Proteins ◽  
Structure Evolution ◽  
Intrinsically Disordered ◽  
Heat Stable ◽  
Temperature Ranges

Proteins possess complex three-dimensional structures, and these structures are stable only within specific ranges of temperature which mostly correspond to the temperature ranges of the host organisms. However, few exceptional proteins, called heat-stable proteins, are stable at temperatures that are substantially higher than those tolerated by the host organisms themselves. Most of the heat-stable proteins possess heat stability to perform their functions at high temperatures, but some of them are intrinsically heat-stable due to their structure. Heat-stable proteins are usually divided into three or four groups depending upon the intricacies of their structures and thermal behaviors. Their peculiar property, i.e. heat-stability, makes them very valuable in applications such as polymerase chain reaction, industrial processes requiring high temperature, and protein engineering. Heat-stability also makes it feasible to purify such proteins, from the rest of the heat-labile proteins, using a simple heat-treatment method. Moreover, heat treatment can be used as a combined cell-lysis and protein purification step which, as compared to conventional methods, can result in a higher yield of heat-stable proteins. Furthermore, some special heat-stable proteins, i.e. intrinsically disordered proteins (which include the proteins involved in important neurodegenerative diseases), need heat-treatment step, in some cases, as the only way for their successful purification and study. Hence, this paper provides a first-ever comprehensive review of all major aspects of heat-stable proteins, i.e., their structure, evolution, classification, significance, and heat-treatment mediated purification.

scholarly journals Preferential adsorption to air–water interfaces: a novel cryoprotective mechanism for LEA proteins

2019 ◽  
Vol 476 (7) ◽  
pp. 1121-1135 ◽  
Author(s):  
Fanny Yuen ◽  
Matthew Watson ◽  
Robert Barker ◽  
Isabelle Grillo ◽  
Richard K. Heenan ◽  
...  
Keyword(s):  
Intrinsically Disordered Proteins ◽  
Citrate Synthase ◽  
Abiotic Stress Tolerance ◽  
Interfacial Area ◽  
Disordered Proteins ◽  
General Mechanism ◽  
Lea Proteins ◽  
Freeze Thaw ◽  
Intrinsically Disordered ◽  
Induced Aggregation

Abstract Late embryogenesis abundant (LEA) proteins comprise a diverse family whose members play a key role in abiotic stress tolerance. As intrinsically disordered proteins, LEA proteins are highly hydrophilic and inherently stress tolerant. They have been shown to stabilise multiple client proteins under a variety of stresses, but current hypotheses do not fully explain how such broad range stabilisation is achieved. Here, using neutron reflection and surface tension experiments, we examine in detail the mechanism by which model LEA proteins, AavLEA1 and ERD10, protect the enzyme citrate synthase (CS) from aggregation during freeze–thaw. We find that a major contributing factor to CS aggregation is the formation of air bubbles during the freeze–thaw process. This greatly increases the air–water interfacial area, which is known to be detrimental to folded protein stability. Both model LEA proteins preferentially adsorb to this interface and compete with CS, thereby reducing surface-induced aggregation. This novel surface activity provides a general mechanism by which diverse members of the LEA protein family might function to provide aggregation protection that is not specific to the client protein.

scholarly journals Plant Dehydrins: Expression, Regulatory Networks, and Protective Roles in Plants Challenged by Abiotic Stress

2021 ◽  
Vol 22 (23) ◽  
pp. 12619
Author(s):  
Zhenping Sun ◽  
Shiyuan Li ◽  
Wenyu Chen ◽  
Jieqiong Zhang ◽  
Lixiao Zhang ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Regulatory Networks ◽  
Plasma Membranes ◽  
Intrinsically Disordered Proteins ◽  
Plant Stress ◽  
Protective Role ◽  
Late Embryogenesis Abundant ◽  
Disordered Proteins ◽  
Intrinsically Disordered ◽  
Wide Range

Dehydrins, also known as Group II late embryogenesis abundant (LEA) proteins, are classic intrinsically disordered proteins, which have high hydrophilicity. A wide range of hostile environmental conditions including low temperature, drought, and high salinity stimulate dehydrin expression. Numerous studies have furnished evidence for the protective role played by dehydrins in plants exposed to abiotic stress. Furthermore, dehydrins play important roles in seed maturation and plant stress tolerance. Hence, dehydrins might also protect plasma membranes and proteins and stabilize DNA conformations. In the present review, we discuss the regulatory networks of dehydrin gene expression including the abscisic acid (ABA), mitogen-activated protein (MAP) kinase cascade, and Ca2+ signaling pathways. Crosstalk among these molecules and pathways may form a complex, diverse regulatory network, which may be implicated in regulating the same dehydrin.

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

Biomolecules ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 1662
Author(s):  
Mughair Abdul Aziz ◽  
Miloofer Sabeem ◽  
Sangeeta Kutty Mullath ◽  
Faical Brini ◽  
Khaled Masmoudi
Keyword(s):  
Intrinsically Disordered Proteins ◽  
Association Studies ◽  
Environmental Stresses ◽  
Disordered Proteins ◽  
Genome Wide Association Studies ◽  
Lea Proteins ◽  
Lea Genes ◽  
Intrinsically Disordered ◽  
Wide Range ◽  
Group Ii

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 Phoenix dactylifera 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.

scholarly journals Dry storage of mammalian spermatozoa and cells: state-of-the-art and possible future directions

2021 ◽  
Vol 33 (2) ◽  
pp. 82
Author(s):  
P. Loi ◽  
D. A. Anzalone ◽  
L. Palazzese ◽  
A. Dinnyés ◽  
J. Saragusty ◽  
...  
Keyword(s):  
Intrinsically Disordered Proteins ◽  
State Of The Art ◽  
Relevant Literature ◽  
Late Embryogenesis Abundant ◽  
Disordered Proteins ◽  
Primary Role ◽  
Intrinsically Disordered ◽  
Current State ◽  
Late Embryogenesis ◽  
The Right

This review provides a snapshot of the current state-of-the-art of drying cells and spermatozoa. The major successes and pitfalls of the most relevant literature are described separately for spermatozoa and cells. Overall, the data published so far indicate that we are closer to success in spermatozoa, whereas the situation is far more complex with cells. Critical for success is the presence of xeroprotectants inside the spermatozoa and, even more so, inside cells to protect subcellular compartments, primarily DNA. We highlight workable strategies to endow gametes and cells with the right combination of xeroprotectants, mostly sugars, and late embryogenesis abundant (LEA) or similar ‘intrinsically disordered’ proteins to help them withstand reversible desiccation. We focus on the biological aspects of water stress, and in particular cellular and DNA damage, but also touch on other still unexplored issues, such as the choice of both dehydration and rehydration methods or approaches, because, in our view, they play a primary role in reducing desiccation damage. We conclude by highlighting the need to exhaustively explore desiccation strategies other than lyophilisation, such as air drying, spin drying or spray drying, ideally with new prototypes, other than the food and pharmaceutical drying strategies currently used, tailored for the unique needs of cells and spermatozoa.

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