The heat‐shock protein/chaperone network and multiple stress resistance

Jacob, Pierre; Hirt, Heribert; Bendahmane, Abdelhafid

doi:10.1111/pbi.12659

Cited by 496 publications

(322 citation statements)

References 109 publications

(142 reference statements)

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“…Heat shock proteins function as molecular chaperones and can reduce -and even prevent -the aggregation of proteins damaged by heat or other stresses, and can assist in the refolding or degradation of stress-damaged proteins. 58 Small HSPs (sHSPs; 15-42 kDa) accumulate in response to various stresses under the transcriptional regulation of HSFs, 59 and it was recently demonstrated that several sHSPs were strongly induced by postharvest cold stress in a chilling-tolerant tomato cultivar, but not in a chilling-sensitive one. 60 Similarly, our present data reveal a significant induction of a 17.3 kDa HSP transcript in all chilling-tolerant pomegranate fruits but not in chilling-sensitive ones ( Table 1).…”

Section: Stressmentioning

confidence: 99%

Molecular mechanisms involved in postharvest chilling tolerance of pomegranate fruit

2019

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Cold storage of pomegranates is essential for prolonging postharvest storage and for the implementation of cold‐quarantine insect disinfestation treatments required for international trading. However, pomegranates are chilling sensitive; they may develop chilling injuries upon exposure to unfavorable low temperatures. In this mini‐review, we summarize molecular data obtained from three different RNA Seq transcriptome analyses of responses of pomegranate fruits to cold storage. These experiments included comparisons among the transcriptomic responses following a 2‐week exposure to 1 °C in three different model systems: 1) unconditioned chilling‐sensitive fruits versus relatively chilling‐tolerant low‐temperature‐conditioned fruits; 2) chilling‐sensitive early harvested fruits versus relatively chilling‐tolerant late‐harvested ones; and 3) chilling‐sensitive ‘Ganesh’ variety versus the relatively chilling‐tolerant ‘Wonderful’ variety. Comparisons among differentially expressed transcripts that were exclusively and significantly up‐regulated in the relatively chilling‐tolerant fruits in all three model systems enabled identification of 573 common chilling tolerance‐associated genes in pomegranates. Functional categorization and classification of the differentially expressed transcripts revealed several regulatory, metabolic, and stress‐adaptation pathways that were uniquely activated in response to cold storage in relatively chilling‐tolerant fruits. More specifically, we identified common up‐regulation of transcripts involved in activation of jasmonic acid and ethylene hormone biosynthesis and signaling, stress‐related transcription factors, calcium and MAPK signaling, starch degradation and galactinol and raffinose biosynthesis, phenol biosynthesis, lipid metabolism, and heat‐shock proteins. We hypothesized these pathways to be involved in imparting chilling tolerance to pomegranate fruits. © 2019 Society of Chemical Industry

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Section: Stressmentioning

confidence: 99%

Molecular mechanisms involved in postharvest chilling tolerance of pomegranate fruit

2019

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“…Of all the changes associated with MHR A. fatua discussed above, perhaps the most intriguing is the constitutive reduction of HSP transcripts and proteins and altered HSP PTM patterns . In all eukaryotes, HSPs are typically induced and subjected to PTMs in response to heat shock as well as a wide variety of biotic and abiotic stresses, and they are implicated in hormetically induced epigenetic effects on phenotype . HSPs primarily function as molecular chaperones that repair misfolded client proteins during stress, although a subset regulate transcription factors for a diverse set of genes .…”

Section: Ntsr: a Role For Heat Shock Proteins?mentioning

confidence: 99%

“…Experimental evidence shows that pharmacologic reductions of HSP90 levels in Drosophila and Arabidopsis produced a wide variety of novel phenotypes, and the same treatment in S. cerevisiae and Candida albicans led to the evolution of resistance to two classes of fungicides . The role of HSP90 as a global regulator of diverse stress‐induced signaling pathways is now well accepted . The results from MHR A. fatua plants indicate that a very different stress, i.e.…”

Section: Ntsr: a Role For Heat Shock Proteins?mentioning

confidence: 99%

Stress‐induced evolution of herbicide resistance and related pleiotropic effects

Dyer

2018

Pest Management Science

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Herbicide-resistant weeds, especially those with resistance to multiple herbicides, represent a growing worldwide threat to agriculture and food security. Natural selection for resistant genotypes may act on standing genetic variation, or on a genetic and physiological background that is fundamentally altered because of stress responses to sublethal herbicide exposure. Stress-induced changes include DNA mutations, epigenetic alterations, transcriptional remodeling, and protein modifications, all of which can lead to herbicide resistance and a wide range of pleiotropic effects. Resistance selected in this manner is termed systemic acquired herbicide resistance, and the associated pleiotropic effects are manifested as a suite of constitutive transcriptional and post-translational changes related to biotic and abiotic stress adaptation, representing the evolutionary signature of selection. This phenotype is being investigated in two multiple herbicide-resistant populations of the hexaploid, self-pollinating weedy monocot Avena fatua that display such changes as well as constitutive reductions in certain heat shock proteins and their transcripts, which are well known as global regulators of diverse stress adaptation pathways. Herbicide-resistant populations of most weedy plant species exhibit pleiotropic effects, and their association with resistance genes presents a fertile area of investigation. This review proposes that more detailed studies of resistant A. fatua and other species through the lens of plant evolution under stress will inform improved resistant weed prevention and management strategies. © 2018 Society of Chemical Industry.

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“…Chaperones play a pivotal role in protein quality control, ensuring the correct folding of proteins, the refolding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (Hartl and Hayer‐Hartl ). Heat shock proteins (HSPs) act as molecular chaperones that protect plants against various stresses by re‐establishing normal protein conformation and cellular homeostasis (Wang et al , Jacob et al ). The 70 kDa HSP (spot 2815) was found to be upregulated with the increase of exogenous BAP concentration, which might prevent protein misfolding and aggregating during tuber development.…”

Section: Discussionmentioning

confidence: 99%

An integrative overview of physiological and proteomic changes of cytokinin‐induced potato (Solanum tuberosum L.) tuber development in vitro

Cheng

Wang

et al. 2019

Physiologia Plantarum

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Potato tuberization is a complicated biological process regulated by multiple phytohormones, in particular cytokinins (CKs). The information available on the molecular mechanisms regulating tuber development by CKs remains largely unclear. Physiological results initially indicated that low 6‐benzylaminopurine (BAP) concentration (3 mg l−1) advanced the tuberization beginning time and promoted tuber formation. A comparative proteomics approach was applied to investigate the proteome change of tuber development by two‐dimensional gel electrophoresis in vitro, subjected to exogenous BAP treatments (0, 3, 6 and 13 mg l−1). Quantitative image analysis showed a total of 83 protein spots with significantly altered abundance (>2.5‐fold, P < 0.05), and 55 differentially abundant proteins were identified by MALDI‐TOF/TOF MS. Among these proteins, 22 proteins exhibited up‐regulation with the increase of exogenous BAP concentration, and 31 proteins were upregulated at 3 mg l−1 BAP whereas being downregulated at higher BAP concentrations. These proteins were involved in metabolism and bioenergy, storage, redox homeostasis, cell defense and rescue, transcription and translation, chaperones, signaling and transport. The favorable effects of low BAP concentrations on tuber development were found in various cellular processes, mainly including the stimulation of starch and storage protein accumulation, the enhancement of the glycolysis pathway and ATP synthesis, the cellular homeostasis maintenance, the activation of pathogen defense, the higher efficiency of transcription and translation, as well as the enhanced metabolite transport. However, higher BAP concentration, especially 13 mg l−1, showed disadvantageous effects. The proposed hypothetical model would explain the interaction of these proteins associated with CK‐induced tuber development in vitro.

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The heat‐shock protein/chaperone network and multiple stress resistance

Cited by 496 publications

References 109 publications

Molecular mechanisms involved in postharvest chilling tolerance of pomegranate fruit

Molecular mechanisms involved in postharvest chilling tolerance of pomegranate fruit

Stress‐induced evolution of herbicide resistance and related pleiotropic effects

An integrative overview of physiological and proteomic changes of cytokinin‐induced potato (Solanum tuberosum L.) tuber development in vitro

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