Genome-wide identification and expression profiling of the dehydrin gene family in Actinidia chinensis

Zhang, Jun; Xia, Hui; Liang, Dong; Lin, Lijin; Deng, Honghong; Lv, Xiulan; Wang, Zhihui; Zhang, Xiao'ai; Wang, Jin; Xiong, Bo

doi:10.1016/j.scienta.2021.109930

Cited by 2 publications

(4 citation statements)

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“…These genes were highly expressed in stems, leaves, roots, and fruits. During the leaf growth, the expression levels of some of these genes were downregulated, and during fruit growth, they were upregulated [66]. These findings suggested that group II LEA genes also play a role in the regulation of leaf or fruit development [66].…”

Section: Genome-wide Association Studies (Gwas) Of Group II Lea Proteinsmentioning

confidence: 94%

“…During the leaf growth, the expression levels of some of these genes were downregulated, and during fruit growth, they were upregulated [66]. These findings suggested that group II LEA genes also play a role in the regulation of leaf or fruit development [66]. However, under the different abiotic stresses of salinity, drought, and high and low temperatures, the transcription levels of these genes were significantly increased.…”

Section: Genome-wide Association Studies (Gwas) Of Group II Lea Proteinsmentioning

confidence: 98%

“…The group II LEA genes of Sorghum displayed one ortholog with Oryza sativa and Zea mays and three with Setaria italica, whereas Sorghum bicolor group II LEA genes encoded for ordered proteins that possessed many phosphorylation sites [65]. In another GWAS, seven group II LEA genes were identified in Actinidia chinensis that belonged to putative proteins of YSK and SK groups [66]. These genes were highly expressed in stems, leaves, roots, and fruits.…”

Section: Genome-wide Association Studies (Gwas) Of Group II Lea Proteinsmentioning

confidence: 99%

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

et al. 2021

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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.

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Section: Genome-wide Association Studies (Gwas) Of Group II Lea Proteinsmentioning

confidence: 94%

Section: Genome-wide Association Studies (Gwas) Of Group II Lea Proteinsmentioning

confidence: 98%

Section: Genome-wide Association Studies (Gwas) Of Group II Lea Proteinsmentioning

confidence: 99%

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

et al. 2021

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“…However, several studies have analyzed the genomes of various plants (rice, wheat, kiwi, locoweed, potatoes) with the intention of identifying the dehydrins and creating phylogenetic trees in order to better understand their evolution within that plant. These studies often conclude that tandem and/or segmental duplication are major factors in the diversification of the dehydrin family [ 31 , 32 , 33 , 34 , 35 ]. One of the more comprehensive family-oriented studies focused on the Pinaceae family, where the authors identified the N1-segment, which is now known as the F-segment [ 36 ].…”

Section: Evolution Of Dehydrinsmentioning

confidence: 99%

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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Genome-wide identification and expression profiling of the dehydrin gene family in Actinidia chinensis

Cited by 2 publications

References 44 publications

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

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

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

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