Universal Stress Protein Exhibits a Redox-Dependent Chaperone Function in Arabidopsis and Enhances Plant Tolerance to Heat Shock and Oxidative Stress (original) (raw)
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Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
Trends in Plant Science, 2004
Abiotic stresses usually cause protein dysfunction. Maintaining proteins in their functional conformations and preventing the aggregation of non-native proteins are particularly important for cell survival under stress. Heat-shock proteins (Hsps)/chaperones are responsible for protein folding, assembly, translocation and degradation in many normal cellular processes, stabilize proteins and membranes, and can assist in protein refolding under stress conditions. They can play a crucial role in protecting plants against stress by reestablishing normal protein conformation and thus cellular homeostasis. Here, we summarize the significance of Hsps and chaperones in abiotic stress responses in plants, and discuss the co-operation among their different classes and their interactions with other stressinduced components.
Plant signaling & behavior
Oxidative stress, arising from an imbalance in the generation and removal of reactive oxygen species (ROS), is a challenge faced by all aerobic organisms. In plants, different pathways sense ROS from extracellular sources or organelles such as mitochondria, chloroplast or peroxisome. In our recent paper on Plant Molecular Biology1 we have studied the Arabidopsis thaliana early response to the generation of superoxide anion in chloroplasts during active photosynthesis. Transcript profile analysis revealed that the expression level of various genes encoding heat shock proteins (Hsps), increased after a short term of oxidative stress treatment. Furthermore, there was an induction of heat shock transcription factors HsfA2 and HsfA4A that were reported to be regulators of genes involved in stress response of Arabidopsis.1,2In this addendum, we complement the expression analysis of two Hsp genes encoding Hsp70 and a 17.6 kDa class I small heat-shock protein (sHsp), and discuss their plaus...
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.
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
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.
Heat Shock Factors: Regulators of Early and Late Functions in Plant Stress Response
Heat shock factors (HSFs) among others are of great importance regarding the regulation of increased stress tolerance. Based on structural characteristics and phylogenetic comparison plant HSFs are subdivided into 3 classes and several subgroups. Recent studies showed that different HSFs play important roles during early and late stages of stress response. In this review, we focus mainly on the functional characterisation of class A HSFs of Arabidopsis, which are known to function as transcriptional activators of stress target genes. Recent evidence obtained from the identification of HSF-knockout mutants and microarray expression profiling indicates that different early and late HSF regulate large numbers of partially overlapping sets of target genes. Meta-analysis of microarray data generated from different experimental setup may have the potential to verify known and/or to identify novel HSF target genes. In addition, we will summarise recent work on the potential roles of oxidative stress leading to the activation of HSFs and the induction of the heat stress response. _____________________________________________________________________________________________________________ Keywords: electrophoretic mobility shift assay, heat stress, knock out mutants, microarray, oxidative stress CONTENTS
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.