Research advances in function and regulation mechanisms of plant small heat shock proteins (sHSPs) under environmental stresses

Wu, Jieting; Gao, Tian; Hu, Jianing; Zhao, Lei; Yu, Chang Yeon; Ma, Fengwang

doi:10.1016/j.scitotenv.2022.154054

Cited by 58 publications

(41 citation statements)

References 142 publications

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“…These CrHsp20s may act as molecular chaperones to protect yeast against heat stress damage by stabilizing proteins and membranes from degeneration, thereby maintaining regular yeast growth. Although some reports indicated that plant Hsp20s may also reduce the toxic effects of abiotic stresses by scavenging cellular ROS indirectly [ 24 , 38 , 47 ], and RcHSP17.8 in rose could enhance yeast H 2 O 2 tolerance after overexpression, in our study we found that none of these seven CrHsp20s could elevate the H 2 O 2 tolerance in either the skn7Δ or yap1Δ yeast mutant strains ( Figure 10 ). This is quite different from other antioxidant molecular chaperones, such as late embryogenesis abundant (LEA) and abscisic acid-, stress-, and ripening-induced (ASR) proteins [ 54 ], or metallothioneins (MTs) [ 39 ].…”

Section: Discussioncontrasting

confidence: 71%

“…Oxidative stress caused by the increased accumulation of reactive oxygen species (ROS), such as H 2 O 2 and superoxide anion, is the consequence of many cellular metabolic processes and biotic/abiotic stresses. Hsp20s have significant effects on the response to oxidative stress [ 38 ]. Here we also assessed the possible antioxidant abilities of seven CrHsp20s with a yeast spot assay.…”

Section: Resultsmentioning

confidence: 99%

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Comprehensive Analysis of the Hsp20 Gene Family in Canavalia rosea Indicates Its Roles in the Response to Multiple Abiotic Stresses and Adaptation to Tropical Coral Islands

Zhang

Jian

Wang

2022

IJMS

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Heat shock protein 20 (Hsp20) is a major family of heat shock proteins that mainly function as molecular chaperones and are markedly accumulated in cells when organisms are subjected to environmental stress, particularly heat. Canavalia rosea is an extremophile halophyte with good adaptability to environmental high temperature and is widely distributed in coastal areas or islands in tropical and subtropical regions. In this study, we identified a total of 41 CrHsp20 genes in the C. rosea genome. The gene structures, phylogenetic relationships, chromosome locations, and conserved motifs of each CrHsp20 or encoding protein were analyzed. The promoters of CrHsp20s contained a series of predicted cis-acting elements, which indicates that the expression of different CrHsp20 members is regulated precisely. The expression patterns of the CrHsp20 family were analyzed by RNA sequencing both at the tissue-specific level and under different abiotic stresses, and were further validated by quantitative reverse transcription PCR. The integrated expression profiles of the CrHsp20s indicated that most CrHsp20 genes were greatly upregulated (up to dozens to thousands of times) after 2 h of heat stress. However, some of the heat-upregulated CrHsp20 genes showed completely different expression patterns in response to salt, alkaline, or high osmotic stresses, which indicates their potential specific function in mediating the response of C. rosea to abiotic stresses. In addition, some of CrHsp20s were cloned and functionally characterized for their roles in abiotic stress tolerance in yeast. Taken together, these findings provide a foundation for functionally characterizing Hsp20s to unravel their possible roles in the adaptation of this species to tropical coral reefs. Our results also contribute to the understanding of the complexity of the response of CrHsp20 genes to other abiotic stresses and may help in future studies evaluating the functional characteristics of CrHsp20s for crop genetic improvement.

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Section: Discussioncontrasting

confidence: 71%

Section: Resultsmentioning

confidence: 99%

Comprehensive Analysis of the Hsp20 Gene Family in Canavalia rosea Indicates Its Roles in the Response to Multiple Abiotic Stresses and Adaptation to Tropical Coral Islands

Zhang

Jian

Wang

2022

IJMS

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“…Many studies have suggested the importance of HSPs in the crosstalk among cellular response networks activated by different abiotic stresses [ 37 , 38 ]. HSPs are also known to play a pivotal role in cross-stress tolerance, as demonstrated by transgenic plant studies indicating that HSP over-expression implies the activation of other stress response genes, high antioxidant activity, and high osmolyte levels [ 5 , 39 , 40 ].…”

Section: Discussionmentioning

confidence: 99%

Drought Stress Pre-Treatment Triggers Thermotolerance Acquisition in Durum Wheat

Pascali

Caroli

Aprile

et al. 2022

IJMS

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Durum wheat is strongly affected by climatic constraints such as high temperatures and drought, which frequently lead to yield reduction. Damages due to high temperatures are related to plant thermotolerance, a trait determined by two components: basal and acquired thermotolerance. In this study, the effect of drought and heat stress imposed singularly or sequentially was investigated in ten durum wheat cultivars (cvs) at the physiological and molecular level. The traits analyzed were cell membrane stability, relative water content, proline content, and expression level of several genes for heat shock proteins (HSPs). Our results indicate that drought priming can induce the acquisition of thermotolerance in most cultivars already classified as able to acquire thermotolerance by heat pre-treatment. Proline accumulation was correlated to cell membrane stability, meaning that the most thermotolerant cvs were able to accumulate higher levels of proline. Acquired thermotolerance is also due to the activation of HSP gene expression; similarly, pre-treatment with water stress was able to activate HSPs expression. The results reported indicate that water stress plays an important role in inducing thermotolerance, comparable to mild heat stress pre-treatment. This is the first report on the effect of drought stress on the acquisition of thermotolerance.

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“…Highly disordered tudor staphylococcal nuclease (TSN) associating with stress granule proteins via its N-terminal IDR acts a docking platform for a protein–protein interaction network to enable rapid stress granule assembly under stress (Gutierrez-Beltran et al, 2021 ). Small heat shock proteins (sHSPs) protect cells against stress-induced cell damage by binding to and maintaining denaturing proteins in a folding-competent state (Wu et al, 2022 ). The N-terminal IDR of pea sHsp18.1 presents a variable and flexible ensemble with multiple binding site conformations; hence, sHSPs are highly effective in interacting in a wide range of different cellular proteins (Jaya et al, 2009 ).…”

Section: Conformational Flexibility Enables Broad Specificitymentioning

confidence: 99%

Plant Protein Disorder: Spatial Regulation, Broad Specificity, Switch of Signaling and Physiological Status

Hsiao

2022

Front. Plant Sci.

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Research advances in function and regulation mechanisms of plant small heat shock proteins (sHSPs) under environmental stresses

Cited by 58 publications

References 142 publications

Comprehensive Analysis of the Hsp20 Gene Family in Canavalia rosea Indicates Its Roles in the Response to Multiple Abiotic Stresses and Adaptation to Tropical Coral Islands

Comprehensive Analysis of the Hsp20 Gene Family in Canavalia rosea Indicates Its Roles in the Response to Multiple Abiotic Stresses and Adaptation to Tropical Coral Islands

Drought Stress Pre-Treatment Triggers Thermotolerance Acquisition in Durum Wheat

Plant Protein Disorder: Spatial Regulation, Broad Specificity, Switch of Signaling and Physiological Status

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