F-segments of Arabidopsis dehydrins show cryoprotective activities for lactate dehydrogenase depending on the hydrophobic residues

Ohkubo, Tomohiro; Kameyama, Ayuko; Kamiya, Keita; Kondo, Mitsuru; Hara, Masakazu

doi:10.1016/j.phytochem.2020.112300

Cited by 16 publications

(17 citation statements)

References 44 publications

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“…The AtHIRD11 His residue protected LDH against inactivation by heavy metals [ 122 ]. The hydrophobic residues of the F-segments in Arabidopsis COR47 (FSKn-type dehydrin) protected LDH against inactivation by freezing [ 123 ]. Thus, dehydrins are multifunctional enzyme protectors and improve plant stress resistance [ 124 ].…”

Section: Functional Diversity Of Dehydrinsmentioning

confidence: 99%

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

Sun

Chen

et al. 2021

IJMS

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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.

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Section: Functional Diversity Of Dehydrinsmentioning

confidence: 99%

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

Sun

Chen

et al. 2021

IJMS

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“…This includes conservation in the K- and F-segments of their hydrophobic character, which plays important roles in the cryoprotective activities of dehydrins. Previous reports focused on the truncated forms of the F- and K-segments have shown their involvement in enzyme protection [ 35 , 41 , 57 , 58 , 59 ]. This is not surprising, since these mechanisms are likely similar between halophytes and glycophytes, such that the sequences must be fairly conserved.…”

Section: Resultsmentioning

confidence: 99%

The Halophyte Dehydrin Sequence Landscape

2022

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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.

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“…Dehydrins have been implicated in protein cryoprotection from freezing stress in many studies [ 41 , 50 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 73 , 74 , 75 , 76 ]. The most commonly used enzyme is lactate dehydrogenase (LDH), a cold-labile protein that denatures and loses almost all activity after freeze-thaw stress, although other enzymes such as malate dehydrogenase and alcohol dehydrogenase have been tested [ 50 , 60 , 77 , 78 , 79 , 80 , 81 ].…”

Section: Protein Cryoprotectionmentioning

confidence: 99%

“…There has been considerable interest in the field when it comes to trying to understand what role the conserved segments may have in protecting LDH from freeze/thaw damage. There have been reports of the K-segment (and more recently, the F-segment) being involved in cryoprotection of LDH by using 15-residue peptides of these segments in the freeze/thaw assay [ 73 , 76 ]. Intriguingly, in the case of both motifs the hydrophobic residues were shown to play an essential role in this cryoprotective effect.…”

Section: Protein Cryoprotectionmentioning

confidence: 99%

“…Intriguingly, in the case of both motifs the hydrophobic residues were shown to play an essential role in this cryoprotective effect. The hydrophobic residues were determined to form solvent-exposed hydrophobic patches (four residues splayed out in different directions in the F-segment, or an amphipathic helix in the K-segment) using PEP-FOLD3 [ 73 , 76 ]. The authors proposed that these hydrophobic patches may then intercalate between LDH molecules that are beginning to denature, transiently interact with the hydrophobic regions, and keep the LDH from aggregating, which allows the enzyme surface to undergo ‘hydrophobic hydration’ [ 76 ].…”

Section: Protein Cryoprotectionmentioning

confidence: 99%

See 1 more Smart Citation

The Disordered Dehydrin and Its Role in Plant Protection: A Biochemical Perspective

Smith

Graether

2022

Biomolecules

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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.

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F-segments of Arabidopsis dehydrins show cryoprotective activities for lactate dehydrogenase depending on the hydrophobic residues

Cited by 16 publications

References 44 publications

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

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

The Halophyte Dehydrin Sequence Landscape

The Disordered Dehydrin and Its Role in Plant Protection: A Biochemical Perspective

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