Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response (original) (raw)
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Journal of Bioresource Management, 2021
Heat shock proteins assist in folding proteins that is a basic cellular constituent responsible for various crucial functions including protein assembly, transportation, folding in normal conditions and denaturation of proteins in stress and in other cellular function. Abiotic factors like increased temperature, drought and salinity negatively affect reproduction and survival of plants. Plants (HSPs), as chaperones, have crucial part in conversing biotic and abiotic stress tolerance. Plants react towards critical changes through biochemical, growth, and physiological mechanisms included expression of stress-reactive proteins, which are regulated by interconnected signaling cascades of transcription factors including heat stress TFs.
Role of Heat Shock Proteins in Improving Heat Stress Tolerance in Crop Plants
Heat Shock Proteins, 2016
High temperature response (HTR) or heat stress response (HSR) is a highly conserved phenomenon, which involves complex networks among different crop species. Heat stress usually results in protein dysfunction by improper folding of its linear amino acid chains to non-native proteins. This leads to unfavourable interactions and subsequent protein aggregation. To tackle this, plants have developed molecular chaperone machinery to maintain high quality proteins in the cell. This is governed by increasing the level of pre-existing molecular chaperones and by expressing additional chaperones through signalling mechanism. Dissecting the molecular mechanism by which plants counter heat stress and identifi cation of important molecules involved are of high priority. This could help in the development of plants with improved heat stress tolerance through advanced genomics and genetic engineering approaches. Owing to this reason molecular chaperones/Heat shock proteins (Hsps) are considered as potential candidates to address the issue of heat stress. In this chapter, recent progress on systematic analyses of heat shock proteins, their classifi cation and role in plant response to heat stress along with an overview of genomic and transgenic approaches to overcome the issue, are summarized.
International Journal of Innovative Research in Science, Engineering and Technology (IJIRSET), 2024
ABSTRACT: Due to the present scenario of climate change, plants have to evolve strategies to survive and perform under a plethora of biotic and abiotic stresses, which restrict plant productivity. Maintenance of plant protein functional conformation and preventing non-native proteins from aggregation, which leads to metabolic disruption, are of prime importance. Plant heat shock proteins (HSPs), as chaperones, play a pivotal role in conferring biotic and abiotic stress tolerance. Moreover, HSP also enhances membrane stability and detoxifies the reactive oxygen species (ROS) by positively regulating the antioxidant enzymes system. Additionally, it uses ROS as a signal to molecules to induce HSP production. HSP also enhances plant immunity by the accumulation and stability of pathogenesis-related (PR) proteins under various biotic stresses.
Heat Shock Proteins: Functions And Response Against Heat Stress In Plants
Heat stress has significant effect on protein metabolism, including degradation of proteins, inhibition of protein accumulation and induction of certain protein synthesis. It also poses a serious damage to the growth and development of the plant. The ability of the plants to respond to this stress by maintaining protein in their functional conformation as well as preventing the accumulation of non-native proteins are highly important for the cell survival. Heat shock proteins are involved in signaling, translation, host-defence mechanisms, carbohydrate metabolism and amino acid metabolism. In fact, these proteins are now understood to mediate signaling, translation, host-defence mechanisms, carbohydrate metabolism and amino acid metabolism by playing a significant function in controlling the genome and ultimately features that are obvious. Several reviews have reported the tolerance of plants to different abiotic stresses. The topic of enhancing protection mechanisms (including HSPs...
Small heat shock proteins and stress tolerance in plants
Biochimica Et Biophysica Acta-gene Structure and Expression, 2002
Small heat shock proteins (sHsps) are produced ubiquitously in prokaryotic and eukaryotic cells upon heat. The special importance of sHsps in plants is suggested by unusual abundance and diversity. Six classes of sHsps have been identified in plants based on their intracellular localization and sequence relatedness. In addition to heat stress, plant sHsps are also produced under other stress conditions and at certain developmental stages. Induction of sHsp gene expression and protein accumulation upon environmental stresses point to the hypothesis that these proteins play an important role in stress tolerance. The function of sHsps as molecular chaperones is supported by in vitro and in vivo assays. This review summarizes recent knowledge about plant sHsp gene expression, protein structure and functions. D
Plant heat-shock proteins: A mini review
Journal of King Saud University-Science, 2011
Plants as sessile organisms are exposed to persistently changing stress factors. The primary stresses such as drought, salinity, cold and hot temperatures and chemicals are interconnected in their effects on plants. These factors cause damage to the plant cell and lead to secondary stresses such as osmotic and oxidative stresses. Plants cannot avoid the exposure to these factors but adapt morphologically and physiologically by some other mechanisms. Almost all stresses induce the production of a group of proteins called heat-shock proteins (Hsps) or stress-induced proteins. The induction of transcription of these proteins is a common phenomenon in all living things. These proteins are grouped in plants into five classes according to their approximate molecular weight: (1) Hsp100, (2) Hsp90, (3) Hsp70, (4) Hsp60 and (5) small heat-shock proteins (sHsps). Higher plants have at least 20 sHsps and there might be 40 kinds of these sHsps in one plant species. It is believed that this diversification of these proteins reflects an adaptation to tolerate the heat stress. Transcription of heat-shock protein genes is controlled by regulatory proteins called heat stress transcription factors (Hsfs). Plants show at least 21 Hsfs with each one having its role in regulation, but they also cooperate in all phases of periodical heat stress responses (triggering, maintenance and recovery). There are more than 52 plant species (including crop ones) that have been genetically engineered for different traits such as yield, herbicide and insecticide resistance and some metabolic changes.
Heat Shock Proteins and Heat Shock Response in Plants
gazi university journal of science, 2010
Normal 0 21 false false false TR X-NONE X-NONE MicrosoftInternetExplorer4 Prokaryotic and eukaryotic cells respond potentially harmful stimulations like heat stress by inducing synthesis of stress proteins so called heat shock proteins (Hsps) besides other metabolites. Heat stress response is a reaction when tissues and cells of an organism were exposed to sudden heat stress and is characterized by temporary expression of Hsps. Primary protein structures of Hsps and heat shock response are highly conserved in every organism which has been sought. Therefore it has been considered that Hsps might be closely involved in protection of organisms against heat stress and keeping homeostasis. Most of Hsps are known as molecular chaperons whose biological role is to maintain and shield the unfolded state of newly synthesized proteins thus preventing them from misfolding or aggregating. Here it was summarized the significance of Hsps and heat shock response in plants. Key Words : Heat stress...
Frontiers in Plant Science, 2015
Although a wide range of physiological information on Universal Stress Proteins (USPs) is available from many organisms, their biochemical, and molecular functions remain unidentified. The biochemical function of AtUSP (At3g53990) from Arabidopsis thaliana was therefore investigated. Plants over-expressing AtUSP showed a strong resistance to heat shock and oxidative stress, compared with wild-type and Atusp knockout plants, confirming the crucial role of AtUSP in stress tolerance. AtUSP was present in a variety of structures including monomers, dimers, trimers, and oligomeric complexes, and switched in response to external stresses from low molecular weight (LMW) species to high molecular weight (HMW) complexes. AtUSP exhibited a strong chaperone function under stress conditions in particular, and this activity was significantly increased by heat treatment. Chaperone activity of AtUSP was critically regulated by the redox status of cells and accompanied by structural changes to the protein. Over-expression of AtUSP conferred a strong tolerance to heat shock and oxidative stress upon Arabidopsis, primarily via its chaperone function.
Arabidopsis thaliana J-class heat shock proteins: cellular stress sensors
Functional & Integrative Genomics, 2009
Plants are sessile organisms that have evolved a variety of mechanisms to maintain their cellular homeostasis under stressful environmental conditions. Survival of plants under abiotic stress conditions requires specialized group of heat shock protein machinery, belonging to Hsp70:J-protein family. These heat shock proteins are most ubiquitous types of chaperone machineries involved in diverse cellular processes including protein folding, translocation across cell membranes, and protein degradation. They play a crucial role in maintaining the protein homeostasis by reestablishing functional native conformations under environmental stress conditions, thus providing protection to the cell. J-proteins are co-chaperones of Hsp70 machine, which play a critical role by stimulating Hsp70s ATPase activity, thereby stabilizing its interaction with client proteins. Using genome-wide analysis of Arabidopsis thaliana, here we have outlined identification and systematic classification of J-protein co-chaperones which are key regulators of Hsp70s function. In comparison with Saccharomyces cerevisiae model system, a comprehensive domain structural organization, cellular localization, and functional diversity of A. thaliana J-proteins have also been summarized.
Environmental and Experimental Botany, 2018
The roles of three different classes of HSP genes were investigated over control and salt stress conditions. Methodologically, the endogenous HSP genes of N. benthamiana transiently silenced by corresponding heterologous sequences isolated from Capparis spinosa L. using a virus system of gene silencing. Silencing of HSP70, compared to other two HSPs, resulted in stronger negative effects on growth and physiological parameters especially under salinity conditions. Loss of function of molecular chaperones following gene silencing might be partially compensated with a higher accumulation of proline to protect membranes and proteins from stress-related damages. Heat shock proteins (HSPs) have vital roles during plant adaptation to biotic and abiotic stresses, as well as stress-free conditions. In the present study, we used a heterologous strategy of virus induced gene silencing to investigate the role of different classes of HSPs in Nicotiana benthamiana. Different growth and physiological parameters in silenced plants were evaluated under both control and salt stress conditions. Among the treatments, silencing of HSP70, especially under salinity regime, was found to have stronger impacts on growth, protein concentration, the accumulation of photosynthetic pigments, proline and total soluble carbohydrates content, malondialdehyde, the activity of antioxidant enzymes, performance index, relative water content and the ratio of K + /Na + , suggesting a more prominent role for HSP70 in both stressful and stress-free life cycle of the plants. Principal component analysis and hierarchical clustering indicated that HSP70 gene was silenced, the plants might effectively respond to stress by a higher accumulation of compatible solutes, like proline to protect the cell membranes and proteins from damage.