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Biomolecules
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Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection
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Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Cellular Biochemistry".

Deadline for manuscript submissions: closed (15 January 2022) | Viewed by 19271

Special Issue Editor

Prof. Dr. Steffen Graether

E-Mail Website
Guest Editor
Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada
Interests: proteins; intrinsically disordered proteins; protein bioinformatics; protein purification; biophysics; protein expression; protein structure; biochemistry; structural biology; circular dichroism
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Late embryogenesis abundant (LEA) proteins are a group of nine protein families that are able to protect plants from several different forms of abiotic stress, including drought, cold, salinity, and osmotic stresses. They are mostly intrinsically disordered proteins, that is, they do not have a defined structure when alone in solution but often gain some structure when bound to a ligand. A number of studies have shown that LEA proteins are able to protect several types of biomolecules, such proteins, DNA, and membranes, and recent studies suggest that LEA proteins may take part in liquid–liquid phase separation. Other recent studies have explored the structure of LEA proteins in the presence and absence of a ligand. Original manuscripts and reviews dealing with any aspect of LEA proteins and related abiotic stress protection are most welcome.

Prof. Dr. Steffen Graether
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • late embryogenesis abundant (LEA) proteins
  • abiotic stress
  • dehydration-induced proteins (dehydrins)
  • LEA protein structure/function relationship
  • cryoprotection
  • dehydration, intrinsically disordered proteins (IDPs)
  • membrane protection
  • liquid–liquid phase separation

Related Special Issue

Published Papers (6 papers)

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Editorial

Jump to: Research, Review

3 pages, 175 KiB  
Editorial
Proteins Involved in Plant Dehydration Protection: The Late Embryogenesis Abundant Family
by Steffen P. Graether
Biomolecules 2022, 12(10), 1380; https://doi.org/10.3390/biom12101380 - 27 Sep 2022
Cited by 7 | Viewed by 1442
Abstract
Plants have evolved a number of different ways to deal with different types of abiotic stresses; at the molecular level, dehydration can cause multiple forms of damage to different biomolecules [...] Full article
(This article belongs to the Special Issue Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection)

Research

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19 pages, 5401 KiB  
Article
Functional and Conformational Plasticity of an Animal Group 1 LEA Protein
by Brett Janis, Clinton Belott, Tyler Brockman and Michael A. Menze
Biomolecules 2022, 12(3), 425; https://doi.org/10.3390/biom12030425 - 10 Mar 2022
Cited by 12 | Viewed by 3095
Abstract
Group 1 (Dur-19, PF00477, LEA_5) Late Embryogenesis Abundant (LEA) proteins are present in organisms from all three domains of life, Archaea, Bacteria, and Eukarya. Surprisingly, Artemia is the only genus known to include animals that express group 1 LEA proteins in their desiccation-tolerant [...] Read more.
Group 1 (Dur-19, PF00477, LEA_5) Late Embryogenesis Abundant (LEA) proteins are present in organisms from all three domains of life, Archaea, Bacteria, and Eukarya. Surprisingly, Artemia is the only genus known to include animals that express group 1 LEA proteins in their desiccation-tolerant life-history stages. Bioinformatics analysis of circular dichroism data indicates that the group 1 LEA protein AfLEA1 is surprisingly ordered in the hydrated state and undergoes during desiccation one of the most pronounced disorder-to-order transitions described for LEA proteins from A. franciscana. The secondary structure in the hydrated state is dominated by random coils (42%) and β-sheets (35%) but converts to predominately α-helices (85%) when desiccated. Interestingly, AfLEA1 interacts with other proteins and nucleic acids, and RNA promotes liquid–liquid phase separation (LLPS) of the protein from the solvent during dehydration in vitro. Furthermore, AfLEA1 protects the enzyme lactate dehydrogenase (LDH) during desiccation but does not aid in restoring LDH activity after desiccation-induced inactivation. Ectopically expressed in D. melanogaster Kc167 cells, AfLEA1 localizes predominantly to the cytosol and increases the cytosolic viscosity during desiccation compared to untransfected control cells. Furthermore, the protein formed small biomolecular condensates in the cytoplasm of about 38% of Kc167 cells. These findings provide additional evidence for the hypothesis that the formation of biomolecular condensates to promote water stress tolerance during anhydrobiosis may be a shared feature across several groups of LEA proteins that display LLPS behaviors. Full article
(This article belongs to the Special Issue Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection)
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12 pages, 1250 KiB  
Article
The Halophyte Dehydrin Sequence Landscape
by Siwar Ghanmi, Steffen P. Graether and Moez Hanin
Biomolecules 2022, 12(2), 330; https://doi.org/10.3390/biom12020330 - 19 Feb 2022
Cited by 7 | Viewed by 2048
Abstract
Dehydrins (DHNs) belong to the LEA (late embryogenesis abundant) family group II, that comprise four conserved motifs (the Y-, S-, F-, and K-segments) and are known to play a multifunctional role in plant stress tolerance. Based on the presence and order of these [...] Read more.
Dehydrins (DHNs) belong to the LEA (late embryogenesis abundant) family group II, that comprise four conserved motifs (the Y-, S-, F-, and K-segments) and are known to play a multifunctional role in plant stress tolerance. Based on the presence and order of these segments, dehydrins are divided into six subclasses: YnSKn, FnSKn, YnKn, SKn, Kn, and KnS. DHNs are rarely studied in halophytes, and their contribution to the mechanisms developed by these plants to survive in extreme conditions remains unknown. In this work, we carried out multiple genomic analyses of the conservation of halophytic DHN sequences to discover new segments, and examine their architectures, while comparing them with their orthologs in glycophytic plants. We performed an in silico analysis on 86 DHN sequences from 10 halophytic genomes. The phylogenetic tree showed that there are different distributions of the architectures among the different species, and that FSKn is the only architecture present in every plant studied. It was found that K-, F-, Y-, and S-segments are highly conserved in halophytes and glycophytes with a few modifications, mainly involving charged amino acids. Finally, expression data collected for three halophytic species (Puccinillia tenuiflora, Eutrema salsugenium, and Hordeum marinum) revealed that many DHNs are upregulated by salt stress, and the intensity of this upregulation depends on the DHN architecture. Full article
(This article belongs to the Special Issue Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection)
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21 pages, 4309 KiB  
Article
Subcellular Localization of Seed-Expressed LEA_4 Proteins Reveals Liquid-Liquid Phase Separation for LEA9 and for LEA48 Homo- and LEA42-LEA48 Heterodimers
by Orarat Ginsawaeng, Carolin Heise, Rohit Sangwan, Daniel Karcher, Itzell Euridice Hernández-Sánchez, Arun Sampathkumar and Ellen Zuther
Biomolecules 2021, 11(12), 1770; https://doi.org/10.3390/biom11121770 - 25 Nov 2021
Cited by 16 | Viewed by 3635
Abstract
LEA proteins are involved in plant stress tolerance. In Arabidopsis, the LEA_4 Pfam group is the biggest group with the majority of its members being expressed in dry seeds. To assess subcellular localization in vivo, we investigated 11 seed-expressed LEA_4 proteins in embryos [...] Read more.
LEA proteins are involved in plant stress tolerance. In Arabidopsis, the LEA_4 Pfam group is the biggest group with the majority of its members being expressed in dry seeds. To assess subcellular localization in vivo, we investigated 11 seed-expressed LEA_4 proteins in embryos dissected from dry seeds expressing LEA_4 fusion proteins under its native promoters with the Venus fluorescent protein (proLEA_4::LEA_4:Venus). LEA_4 proteins were shown to be localized in the endoplasmic reticulum, nucleus, mitochondria, and plastids. LEA9, in addition to the nucleus, was also found in cytoplasmic condensates in dry seeds dependent on cellular hydration level. Most investigated LEA_4 proteins were detected in 4-d-old seedlings. In addition, we assessed bioinformatic tools for predicting subcellular localization and promoter motifs of 11 seed-expressed LEA_4 proteins. Ratiometric bimolecular fluorescence complementation assays showed that LEA7, LEA29, and LEA48 form homodimers while heterodimers were formed between LEA7-LEA29 and LEA42-LEA48 in tobacco leaves. Interestingly, LEA48 homodimers and LEA42-LEA48 heterodimers formed droplets structures with liquid-like behavior. These structures, along with LEA9 cytoplasmic condensates, may have been formed through liquid-liquid phase separation. These findings suggest possible important roles of LLPS for LEA protein functions. Full article
(This article belongs to the Special Issue Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection)
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Review

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16 pages, 572 KiB  
Review
The Disordered Dehydrin and Its Role in Plant Protection: A Biochemical Perspective
by Margaret A. Smith and Steffen P. Graether
Biomolecules 2022, 12(2), 294; https://doi.org/10.3390/biom12020294 - 11 Feb 2022
Cited by 25 | Viewed by 3417
Abstract
Dehydrins are intrinsically disordered proteins composed of several well conserved sequence motifs known as the Y-, S-, F-, and K-segments, the latter of which is a defining feature of all dehydrins. These segments are interspersed by regions of low sequence conservation and are [...] Read more.
Dehydrins are intrinsically disordered proteins composed of several well conserved sequence motifs known as the Y-, S-, F-, and K-segments, the latter of which is a defining feature of all dehydrins. These segments are interspersed by regions of low sequence conservation and are organized modularly, which results in seven different architectures: Kn, SKn, YnSKn, YnKn, KnS, FnK and FnSKn. Dehydrins are expressed ubiquitously throughout the plant kingdom during periods of low intracellular water content, and are capable of improving desiccation tolerance in plants. In vitro evidence of dehydrins shows that they are involved in the protection of membranes, proteins and DNA from abiotic stresses. However, the molecular mechanisms by which these actions are achieved are as of yet somewhat unclear. With regards to macromolecule cryoprotection, there is evidence to suggest that a molecular shield-like protective effect is primarily influenced by the hydrodynamic radius of the dehydrin and to a lesser extent by the charge and hydrophobicity. The interaction between dehydrins and membranes is thought to be a surface-level, charge-based interaction that may help to lower the transition temperature, allowing membranes to maintain fluidity at low temperatures and preventing membrane fusion. In addition, dehydrins are able to protect DNA from damage, showing that these abiotic stress protection proteins have multiple roles. Full article
(This article belongs to the Special Issue Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection)
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27 pages, 1641 KiB  
Review
Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses
by Mughair Abdul Aziz, Miloofer Sabeem, Sangeeta Kutty Mullath, Faical Brini and Khaled Masmoudi
Biomolecules 2021, 11(11), 1662; https://doi.org/10.3390/biom11111662 - 9 Nov 2021
Cited by 42 | Viewed by 4607
Abstract
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection)
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