The Halophyte Dehydrin Sequence Landscape

Ghanmi, Siwar; Graether, Steffen P.; Hanin, Moez

doi:10.3390/biom12020330

Cited by 11 publications

(7 citation statements)

References 64 publications

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“…Further analysis shows that this position may instead contain histidine or phenylalanine. Note that tryptophan, while aromatic is not found at this position, likely because compared to other aromatic amino acids, it promotes folding ( Barua et al, 2008 ; Ghanmi et al, 2022 ). The F-segment ([EXXDRGXFDFX(G/K)]) is a relatively recently identified motif ( Strimbeck, 2017 ; Riley et al, 2019 ).…”

Section: Dehydrin—a Plant Stress Response Proteinmentioning

confidence: 99%

Physiological, Structural, and Functional Insights Into the Cryoprotection of Membranes by the Dehydrins

Murray

Graether

2022

Front. Plant Sci.

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Plants can be exposed to cold temperatures and have therefore evolved several mechanisms to prevent damage caused by freezing. One of the most important targets are membranes, which are particularly susceptible to cold damage. To protect against such abiotic stresses, plants express a family of proteins known as late embryogenesis abundant (LEA) proteins. Many LEA proteins are intrinsically disordered, that is, they do not contain stable secondary or tertiary structures alone in solution. These proteins have been shown in a number of studies to protect plants from damage caused by cold, drought, salinity, and osmotic stress. In this family, the most studied proteins are the type II LEA proteins, better known as dehydrins (dehydration-induced proteins). Many physiological studies have shown that dehydrins are often located near the membrane during abiotic stress and that the expression of dehydrins helps to prevent the formation of oxidation-modified lipids and reduce the amount of electrolyte leakage, two hallmarks of damaged membranes. One of the earliest biophysical clues that dehydrins are involved in membrane cryoprotection came from in vitro studies that demonstrated a binding interaction between the protein and membranes. Subsequent work has shown that one conserved motif, known as K-segments, is involved in binding, while recent studies have used NMR to explore the residue specific structure of dehydrins when bound to membranes. The biophysical techniques also provide insight into the mechanism by which dehydrins protect the membrane from cold stress, which appears to mainly involve the lowering of the transition temperature.

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Section: Dehydrin—a Plant Stress Response Proteinmentioning

confidence: 99%

Physiological, Structural, and Functional Insights Into the Cryoprotection of Membranes by the Dehydrins

Murray

Graether

2022

Front. Plant Sci.

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“…The α segment is poorly conserved, mainly containing glycine and polar amino acids, which can interact with small molecular polar substances to improve the hydrophilicity of DHN and reduce the damage to proteins. 22 Depending on the presence, deletion, and number of repetitions of these fragments, different combinations of structural domains can be formed, 23 resulting in different taxa, classifying into six subclasses, namely: YnSKn, FnSKn, YnKn, SKn, Kn, and KnS. 24 …”

Section: Introductionmentioning

confidence: 99%

Overexpression of soybean GmDHN9 gene enhances drought resistance of transgenic Arabidopsis

Fan,

Zhang,

Sun

et al. 2024

GM Crops & Food

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Soybean is one of the important oil crops and a major source of protein and lipids. Drought can cause severe soybean yields. Dehydrin protein (DHN) is a subfamily of LEA proteins that play an important role in plant responses to abiotic stresses. In this study, the soybean GmDHN9 gene was cloned and induced under a variety of abiotic stresses. Results showed that the GmDHN9 gene response was more pronounced under drought induction. Subcellular localization results indicated that the protein was localized in the cytoplasm. The role of transgenic Arabidopsis plants in drought stress response was further studied. Under drought stress, the germination rate, root length, chlorophyll, proline, relative water content, and antioxidant enzyme content of transgenic Arabidopsis thaliana transgenic genes were higher than those of wild-type plants, and transgenic plants contained less O 2 − , H 2 O 2 and MDA contents. In short, the GmDHN9 gene can regulate the homeostasis of ROS and enhance the drought resistance of plants.

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“…There are different classes of LEA proteins among which dehydrins (LEA II) is the most studied one. These proteins are generally hydrophilic, thermostable, and highly unstructured 9,16 . Experimentally, dehydrins displayed various functions such as chaperone activity, radical scavengering, membrane protection, protein stabilization, and heavy metal binding 17 .…”

Section: Introductionmentioning

confidence: 99%

“…These proteins are generally hydrophilic, thermostable, and highly unstructured. 9,16 Experimentally, dehydrins displayed various functions such as chaperone activity, radical scavengering, membrane protection, protein stabilization, and heavy metal binding. 17 These biological activities are correlated with the protection of plants against several abiotic stresses.…”

Section: Introductionmentioning

confidence: 99%

The heat‐stable protein fraction from Opuntia ficus‐indica seeds exhibits an enzyme protective effect against thermal denaturation and an antibacterial activity

Drira

Ghanmi

Zaïdi

et al. 2022

Biotech and App Biochem

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Desiccation tolerance in developing seeds occurs through several mechanisms among which, a common group of proteins named dehydrins has received considerable attention. So far, there is no information dealing with the accumulation of dehydrins in seeds of Opuntia ficus‐indica. We have initiated here an extraction protocol based on two critical steps: heat and acid treatments, and the purity of this fraction was analyzed by FTIR spectroscopy. Western blot analysis of the heat‐stable protein fraction (HSF) revealed two main bands of approximately 45 and 44 kDa, while three others of ∼40, 32, and 31 kDa were faintly visible, which were recognized by anti‐dehydrin antibodies. This fraction exhibited a Cu2+‐dependent resistance to protease treatments. Next, we performed a series of assays to compare the functional properties of the HSF with those of the previously characterized wheat dehydrin (DHN‐5). Antibacterial assays revealed that HSF exhibits only moderate antibacterial activities against gram‐negative and gram‐positive bacteria, with a minimum inhibition concentration ranging from 0.25 to 1 mg/ml. However, in vitro assays revealed that compared to DHN‐5, HSF exhibits higher protective activities of the lactate dehydrogenase (LDH) when exposed to heat, freezing, and dehydration stresses. The protective role of HSF seems to be linked to its best ability to minimize protein aggregation.

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The Halophyte Dehydrin Sequence Landscape

Cited by 11 publications

References 64 publications

Physiological, Structural, and Functional Insights Into the Cryoprotection of Membranes by the Dehydrins

Physiological, Structural, and Functional Insights Into the Cryoprotection of Membranes by the Dehydrins

Overexpression of soybean GmDHN9 gene enhances drought resistance of transgenic Arabidopsis

The heat‐stable protein fraction from Opuntia ficus‐indica seeds exhibits an enzyme protective effect against thermal denaturation and an antibacterial activity

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