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

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biomacromolecules: Proteins".

Deadline for manuscript submissions: closed (15 October 2023) | Viewed by 3450

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,

Following a very successful first edition, we are pleased to announce the launch of a second edition of a Special Issue entitled “Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection II”.

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. For the most part, they are intrinsically disordered proteins; 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 as 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 that address any aspect of LEA proteins and their related protection against abiotic stresses 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.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

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

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Related Special Issue

Published Papers (2 papers)

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Research

15 pages, 1875 KiB  
Article
Comparative Analysis of Dehydrins from Woody Plant Species
by Milan Karas, Dominika Vešelényiová, Eva Boszorádová, Peter Nemeček, Zuzana Gerši and Jana Moravčíková
Biomolecules 2024, 14(3), 250; https://doi.org/10.3390/biom14030250 - 20 Feb 2024
Viewed by 1297
Abstract
We conducted analyses on 253 protein sequences (Pfam00257) derived from 25 woody plant species, including trees, shrubs, and vines. Our goal was to gain insights into their architectural types, biochemical characteristics, and potential involvement in mitigating abiotic stresses, such as drought, cold, or [...] Read more.
We conducted analyses on 253 protein sequences (Pfam00257) derived from 25 woody plant species, including trees, shrubs, and vines. Our goal was to gain insights into their architectural types, biochemical characteristics, and potential involvement in mitigating abiotic stresses, such as drought, cold, or salinity. The investigated protein sequences (253) comprised 221 angiosperms (85 trees/shrubs and 36 vines) and 32 gymnosperms. Our sequence analyses revealed the presence of seven architectural types: Kn, KnS, SKn, YnKn, YnSKn, FSKn, and FnKn. The FSKn type predominated in tree and shrub dehydrins of both gymnosperms and angiosperms, while the YnSKn type was more prevalent in vine dehydrins. The YnSKn and YnKn types were absent in gymnosperms. Gymnosperm dehydrins exhibited a shift towards more negative GRAVY scores and Fold Indexes. Additionally, they demonstrated a higher Lys content and lower His content. By analyzing promoter sequences in the angiosperm species, including trees, shrubs, and vines, we found that these dehydrins are induced by the ABA-dependent and light-responsive pathways. The presence of stress- and hormone-related cis-elements suggests a protective effect against dehydration, cold, or salinity. These findings could serve as a foundation for future studies on woody dehydrins, especially in the context of biotechnological applications. Full article
(This article belongs to the Special Issue Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection II)
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16 pages, 3823 KiB  
Article
The Effect of Positive Charge Distribution on the Cryoprotective Activity of Dehydrins
by Margaret A. Smith and Steffen P. Graether
Biomolecules 2022, 12(10), 1510; https://doi.org/10.3390/biom12101510 - 19 Oct 2022
Cited by 4 | Viewed by 1753
Abstract
Dehydrins are intrinsically disordered proteins expressed ubiquitously throughout the plant kingdom in response to desiccation. Dehydrins have been found to have a cryoprotective effect on lactate dehydrogenase (LDH) in vitro, which is in large part influenced by their hydrodynamic radius rather than the [...] Read more.
Dehydrins are intrinsically disordered proteins expressed ubiquitously throughout the plant kingdom in response to desiccation. Dehydrins have been found to have a cryoprotective effect on lactate dehydrogenase (LDH) in vitro, which is in large part influenced by their hydrodynamic radius rather than the order of the amino acids within the sequence (alternatively, this may be a sequence specific effect). However, it seems that a different mechanism may underpin the cryoprotection that they confer to the cold-labile yeast frataxin homolog-1 (Yfh1). Circular dichroism spectroscopy (CD) was used to assess the degree of helicity of Yfh1 at 1 °C, both alone and in the presence of several dehydrin constructs. Three constructs were compared to the wild type: YSK2-K→R (lysine residues substituted with arginine), YSK2-Neutral (locally neutralized charge), and YSK2-SpaceK (evenly distributed positive charge). The results show that sequence rearrangements and minor substitutions have little impact on the ability of the dehydrin to preserve LDH activity. However, when the positive charge of the dehydrin is locally neutralized or evenly distributed, the dehydrin becomes less efficient at promoting structure in Yfh1 at low temperatures. This suggests that a stabilizing, charge-based interaction occurs between dehydrins and Yfh1. Dehydrins are intrinsically disordered proteins, expressed by certain organisms to improve desiccation tolerance. These proteins are thought to serve many cellular roles, such as the stabilization of membranes, DNA, and proteins. However, the molecular mechanisms underlying the function of dehydrins are not well understood. Here, we examine the importance of positive charges in dehydrin sequences by making substitutions and comparing their effects in the cryoprotection of two different proteins. Full article
(This article belongs to the Special Issue Late Embryogenesis Abundant Proteins: Understanding Abiotic Stress Protection II)
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