Importance of heat shock proteins in maize (original) (raw)
Related papers
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.
Journal of Plant Physiology, 1998
Although differences in heat-shock protein (HSP) patterns and differences in heritable drought and/or heat tolerance have been documented, there is no genetic evidence of association of the drought and/or heat tolerance with specific alterations in HSP expression in crop plants. In this study we tested the hypothesis that specific maize HSP(s) is (are) associated with plant ability to withstand soil drying (drought) and heat stress. We previously identified a line of maize, ZPBL 1304, which is tolerant to drought and heat stress and synthesizes a 45 ku (kDa) HSP(s), and a line of maize, ZPL 389, which is sensitive to drought and heat stress and does not synthesize the 45 ku HSP(s) (Ristic et al., 1991). We investigated possible association of the 45 ku HSP(s) of ZPBL 1304 line with the drought and heat tolerance phenotype. The two lines, ZPBL 1304 and ZPL 389, were crossed, and dehydration avoidance, damage to cellular membranes, and pattern of HSP synthesis were investigated in F2 plants after exposure to soil drying and high temperature (45°C) stress conditions. The 45 ku HSP(s) of ZPBL 1304 line was (were) associated with the drought and heat tolerance phenotype. The synthesis of 45 ku HSP(s) was observed in F2 plants that displayed an increased ability to recover from soil drying and heat stress. It is possible that either the 45 ku HSP(s) playa role in recovery from drought and heat stress or their gene(s) are in close proximity to the gene(s) which encode tolerance to drought and heat stress.
Stress Biology
Among the plant molecular mechanisms capable of effectively mitigating the effects of adverse weather conditions, the heat shock proteins (HSPs), a group of chaperones with multiple functions, stand out. At a time of full progress on the omic sciences, they look very promising in the genetic engineering field, especially in order to conceive superior genotypes, potentially tolerant to abiotic stresses (AbSts). Recently, some works concerning certain families of maize HSPs (ZmHSPs) were published. However, there was still a lack of a study that, with a high degree of criteria, would fully conglomerate them. Using distinct but complementary strategies, we have prospected as many ZmHSPs candidates as possible, gathering more than a thousand accessions. After detailed data mining, we accounted for 182 validated ones, belonging to seven families, which were subcategorized into classes with potential for functional parity. In them, we identified dozens of motifs with some degree of simila...
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.
Scientific Reports, 2016
Heat shock proteins (HSPs) perform significant roles in conferring abiotic stress tolerance to crop plants. In view of this, HSPs and their encoding genes were extensively characterized in several plant species; however, understanding their structure, organization, evolution and expression profiling in a naturally stress tolerant crop is necessary to delineate their precise roles in stress-responsive molecular machinery. In this context, the present study has been performed in C 4 panicoid model, foxtail millet, which resulted in identification of 20, 9, 27, 20 and 37 genes belonging to SiHSP100, SiHSP90, SiHSP70, SiHSP60 and SisHSP families, respectively. Comprehensive in silico characterization of these genes followed by their expression profiling in response to dehydration, heat, salinity and cold stresses in foxtail millet cultivars contrastingly differing in stress tolerance revealed significant upregulation of several genes in tolerant cultivar. SisHSP-27 showed substantial higher expression in response to heat stress in tolerant cultivar, and its over-expression in yeast system conferred tolerance to several abiotic stresses. Methylation analysis of SiHSP genes suggested that, in susceptible cultivar, higher levels of methylation might be the reason for reduced expression of these genes during stress. Altogether, the study provides novel clues on the role of HSPs in conferring stress tolerance. Plants in the environment are exposed to several abiotic and biotic stresses which pose serious threat to their survival and productivity; however, plants are evolved with sophisticated molecular machinery to sense and circumvent the stresses. In response to abiotic stresses, plants produce several biomolecules called molecular chaperones, which function in protecting the cells from the adverse impact of stresses. A class of such molecular chaperones are called heat shock proteins (HSP), which are synthesized in response to several stresses including low temperature, osmotic, salinity, oxidative, desiccation, high intensity irradiations, wounding, and heavy metals stresses 1-3. The role of HSPs during stress and unstressed conditions is regulation of protein folding and accumulation along with their localization and degradation 4-7. Nevertheless, the precise role of HSPs in regulating the molecular mechanisms responsible for normal growth and development, and stress response remains elusive 1. In plants, HSPs are classified into five principal classes, namely, HSP100, HSP90, HSP70/DnaK, HSP60/GroE and small heat shock proteins (sHSP) based on their molecular weight 8. In order to delineate the molecular roles of these HSPs, several studies on identification and characterization of HSPs and their corresponding genes were performed in plant species such as Arabidopsis, tomato and rice 6,9-11. In rice, 10, 9, 26 and 29 HSPs were identified belonging to HSP100, HSP90, HSP70, and sHSPs, respectively. Expression profiling of these HSP encoding genes in response to heat, cold, drought and salt stresses showed their differential expression with significant upregulation of sHSP genes during heat stress 6. Identification and expression profiling of sHSP genes in barley during drought stress was reported by Reddy et al. 12. The study identified 20 sHSPs, which are shown to be differentially regulated in response to drought stress. A candidate sHSP protein, Hsp17.5-CI was expressed in E. coli, which
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 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...
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.