Small heat shock proteins: recent developments

Eisenhardt, Benjamin D.

doi:10.1515/bmc-2013-0028

Cited by 18 publications

(14 citation statements)

References 138 publications

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“…Responding to this stimulus, plants synthesized HSPs and chaperone-like proteins in order to restore the correct configuration of proteins and impede aggregation (Wang et al, 2004). sHSPs play important and comprehensive roles in the ability of plants to combat heat stress (Eisenhardt, 2013; Mu et al, 2013). …”

Section: Discussionmentioning

confidence: 99%

The Difference of Physiological and Proteomic Changes in Maize Leaves Adaptation to Drought, Heat, and Combined Both Stresses

et al. 2016

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At the eight-leaf stage, maize is highly sensitive to stresses such as drought, heat, and their combination, which greatly affect its yield. At present, few studies have analyzed maize response to combined drought and heat stress at the eight-leaf stage. In this study, we measured certain physical parameters of maize at the eight-leaf stage when it was exposed to drought, heat, and their combination. The results showed an increase in the content of H2O2 and malondialdehyde (MDA), and in the enzyme activities of superoxide dismutase (SOD), ascorbate peroxidase (APX), and glutathione reductase (GR), but a decrease in the quantum efficiency of photosystem II (ΦPSII). The most obvious increase or decrease in physical parameters was found under the combined stress condition. Moreover, to identify proteins differentially regulated by the three stress conditions at the eight-leaf stage, total proteins from the maize leaves were identified and quantified using multiplex iTRAQ-based quantitative proteomic and LC-MS/MS methods. In summary, the expression levels of 135, 65, and 201 proteins were significantly changed under the heat, drought and combined stress conditions, respectively. Of the 135, 65, and 201 differentially expressed proteins, 61, 28, and 16 responded exclusively to drought stress, heat stress, and combined stress, respectively. Bioinformatics analysis implied that chaperone proteins and proteases play important roles in the adaptive response of maize to heat stress and combined stress, and that the leaf senescence promoted by ethylene-responsive protein and ripening-related protein may play active roles in maize tolerance to combined drought and heat stress. The signaling pathways related to differentially expressed proteins were obviously different under all three stress conditions. Thus, the functional characterization of these differentially expressed proteins will be helpful for discovering new targets to enhance maize tolerance to stress.

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Section: Discussionmentioning

confidence: 99%

The Difference of Physiological and Proteomic Changes in Maize Leaves Adaptation to Drought, Heat, and Combined Both Stresses

et al. 2016

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“…Heat shock proteins (HSPs) have “chaperone-like” activities and accumulate in response to various stresses (Eisenhardt, 2013 ). At least five families of chaperones are found in higher plants: the HSP100 (Clp) family, the HSP90 family, the HSP70 (DnaK) family, chaperonins (GroEL and HSP60), and the small (20–40 kD) HSP (sHSP) family.…”

Section: Discussionmentioning

confidence: 99%

Phosphoproteomic analysis of the response of maize leaves to drought, heat and their combination stress

et al. 2015

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Drought and heat stress, especially their combination, greatly affect crop production. Many studies have described transcriptome, proteome and phosphoproteome changes in response of plants to drought or heat stress. However, the study about the phosphoproteomic changes in response of crops to the combination stress is scare. To understand the mechanism of maize responses to the drought and heat combination stress, phosphoproteomic analysis was performed on maize leaves by using multiplex iTRAQ-based quantitative proteomic and LC-MS/MS methods. Five-leaf-stage maize was subjected to drought, heat or their combination, and the leaves were collected. Globally, heat, drought and the combined stress significantly changed the phosphorylation levels of 172, 149, and 144 phosphopeptides, respectively. These phosphopeptides corresponded to 282 proteins. Among them, 23 only responded to the combined stress and could not be predicted from their responses to single stressors; 30 and 75 only responded to drought and heat, respectively. Notably, 19 proteins were phosphorylated on different sites in response to the single and combination stresses. Of the seven significantly enriched phosphorylation motifs identified, two were common for all stresses, two were common for heat and the combined stress, and one was specific to the combined stress. The signaling pathways in which the phosphoproteins were involved clearly differed among the three stresses. Functional characterization of the phosphoproteins and the pathways identified here could lead to new targets for the enhancement of crop stress tolerance, which will be particularly important in the face of climate change and the increasing prevalence of abiotic stressors.

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“…Small HSPs (Hsp12, Hsp20, Hsp21, and Hsp30) play several roles in the cell which, in general, involve retaining client proteins for further folding by other molecular chaperones [ 23 ]. Hsp12 is required for growth, survival, cell morphology, virulence, and evasion of immune response [ 24 - 26 ].…”

Section: Introductionmentioning

confidence: 99%

Heat Shock Proteins in Dermatophytes: Current Advances and Perspectives

Martinez-Rossi

Jacob²,

Sanches³

et al. 2016

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Heat shock proteins (HSPs) are proteins whose transcription responds rapidly to temperature shifts. They constitute a family of molecular chaperones, involved in the proper folding and stabilisation of proteins under physiological and adverse conditions. HSPs also assist in the protection and recovery of cells exposed to a variety of stressful conditions, including heat. The role of HSPs extends beyond chaperoning proteins, as they also participate in diverse cellular functions, such as the assembly of macromolecular complexes, protein transport and sorting, dissociation of denatured protein aggregates, cell cycle control, and programmed cell death. They are also important antigens from a variety of pathogens, are able to stimulate innate immune cells, and are implicated in acquired immunity. In fungi, HSPs have been implicated in virulence, dimorphic transition, and drug resistance. Some HSPs are potential targets for therapeutic strategies. In this review, we discuss the current understanding of HSPs in dermatophytes, which are a group of keratinophilic fungi responsible for superficial mycoses in humans and animals. Computational analyses were performed to characterise the group of proteins in these dermatophytes, as well as to assess their conservation and to identify DNA-binding domains (5′-nGAAn-3′) in the promoter regions of the hsp genes. In addition, the quantification of the transcript levels of few genes in a pacC background helped in the development of an extended model for the regulation of the expression of the hsp genes, which supports the participation of the pH-responsive transcriptional regulator PacC in this process.

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Small heat shock proteins: recent developments

Cited by 18 publications

References 138 publications

The Difference of Physiological and Proteomic Changes in Maize Leaves Adaptation to Drought, Heat, and Combined Both Stresses

The Difference of Physiological and Proteomic Changes in Maize Leaves Adaptation to Drought, Heat, and Combined Both Stresses

Phosphoproteomic analysis of the response of maize leaves to drought, heat and their combination stress

Heat Shock Proteins in Dermatophytes: Current Advances and Perspectives

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