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Heat stress is considered to induce a wide range of physiological and biochemical changes that cause severe damage to plant cell membrane, disrupt protein synthesis, and affect the efficiency of photosynthetic system by reducing the transpiration due to stomata closure. A brief and mild heat shock is known to induce acquired thermo tolerance in plants that is associated with concomitant production of heat shock proteins’ (HSPs) gene family including HSP70. The findings from different studies by use of technologies have thrown light on the importance of HSP70 to heat, other abiotic stresses and environmental challenges in desserts. There is clear evidence that under heat stress, HSP70 gene stabilized the membrane structure, chlorophyll and water breakdown. It was also found that under heat stress, HSP70 decreased the malondialdehyde (MDA) content and increased the production of superoxide dismutase (SOD) and peroxidase (POD) in transgenic plants as compared to non-transgenic plants. Some reactive oxygen species (ROS) such as superoxide, hydrogen peroxide and hydroxyl radical are also synthesized and accumulated when plants are stressed by heat. Hence HSP70 can confidently be used for transforming a number of heat tolerant crop species.
University of the Punjab Lahore, Centre of Excellence in Molecular Biology, Pakistan
Batcho Anicet Agossa
University of the Punjab Lahore, Centre of Excellence in Molecular Biology, Pakistan
Faculty of Agriculture and Environmental Sciences, Catholic University of the West Africa Cotonou, Benin
Zainab Y. Sandhu
Montclair State University, USA
Muhammad Bilal Sarwar
University of the Punjab Lahore, Centre of Excellence in Molecular Biology, Pakistan
Sameera Hassan
University of the Punjab Lahore, Centre of Excellence in Molecular Biology, Pakistan
Bushra Rashid
University of the Punjab Lahore, Centre of Excellence in Molecular Biology, Pakistan
*Address all correspondence to: fatima.batool@cemb.edu.pk
1. Introduction
Heat Shock Proteins (HSPs) are a family of functionally associated proteins which regulates their expression when cells are subjected to high temperatures or other stimuli [1]. As intracellular chaperones, HSP genes are an evolutionarily conserved class of proteins in all living organisms, from bacteria to humans. They are important components that contribute to cellular homeostasis under favorable and harmful growth conditions in prokaryotic and eukaryotic cells [2]. They are responsible for the folding, assembly, translocation and degradation of proteins during normal cell growth and development. Many HSP members perform critically important chaperone roles, such as three-dimensional folding of newly formed proteins and/or proteins weakened by cell stress [3]. For this reason, many chaperones are known to be HSPs due to their existence as aggregates when denatured by heat stress. Under high temperature conditions, their expression levels are increased by transcription of heat shock transcription factors (HSTFs) which are enabled by trimerization of their monomeric forms. This gene regulation system of HSPs is one of the most defined response systems known at molecular level for organisms exposed to extreme temperature conditions [4]. Based on their respective molecular weights, HSPs are referred to small HSP (HSP18, HSP20 and HSP40) and large HSP (HSP60, HSP70, HSP90 and HSP100) [5].
HSP70s are an essential part of the cellular protein folding mechanism and help the cells to defend against stress. Strongly regulated by heat stress, their mechanism interacts with expanded protein peptide segments as well as partly folded proteins to resist aggregation, reshape folding pathways, and regulate activity [6]. When there is no interaction with peptide substrate, HSP70 is normally ATP (Adenosine 5′-triphosphate) bound, distinguished by very poor ATPase activity. When newly synthesized proteins emerge from the ribosomes, the HSP70 substrate binding domain identifies and interacts with hydrophobic amino acid residue sequences [7]. Ubiquitously found in all living species, they inhibit aggregation and assist in the reproduction of non-active proteins in both normal and stress conditions and provide heat-tolerance in plants that are under heat stress. They also inhibit protein folding in mitochondria/chloroplast during post-translational importation. They are also involved in the import and translocation mechanism of proteins and promote the proteolytic degradation of defective proteins by transferring these proteins to lysosomes or proteasomes [8]. The key role is to manage protein folding and quality control in a crowded cell environment. It also plays a crucial role in signal transduction networks, cell cycle regulation, protein degradation and protein trafficking. In addition, it may also play a role in the morphological evolution and adaptation to stress. They were isolated from the cytosol, the endoplasmic reticulum and the plastid of many plants [9]. Recent studies have shown that HSP70 interacts with the 26S proteasome and plays a crucial function in its assembly and maintenance. As the most abundant proteins in the cells, HSP70 genes have been recorded in many plant species, such as Arabidopsis, soybean, tobacco, rice, maize wheat and Agave [10, 11]. They are also constitutively expressed in plants but their expression is developmentally regulated and caused by various environmental factors such as drought, cold, high temperature and salt. Studies have shown their involvement in cytosols, mitochondria and chloroplasts, play an important role in remodeling machines that contribute to preserving the integrity of the cell proteome by promoting protein remodeling, disaggregation, reactivation and degradation of malformed and inactive proteins [12]. The mechanism for the recovery of proteins from aggregation often requires the assistance of another ATP-dependent chaperone system. The HSP70 family solubilizes the aggregated protein and extracts it in a process that can be repeated with the aid of a specific HSP family of genes [13]. This review focuses on recent discoveries of molecular and cellular mechanisms of HSP70 that govern the tolerance of plants in unfavorable environmental conditions.
2. Biochemical and physiological responses of plants against heat stress
Heat inducible genes can be categorized in two agencies. The primary organization consists of proteins that maximum probably characteristic in abiotic stress tolerance. These encompass molecules along with antifreeze proteins, chaperones osmotin, late embryogenesis abundant (LEA) proteins, mRNA-binding proteins, key enzymes involved in osmolyte biosynthesis, proteins of water channel, transporters like sugars and proline, detoxification enzymes and numerous proteases. The second institution consists of regulatory proteins i.e. protein factors concerned in addition law of signal transduction and stress-responsive gene expression [14, 15]. These encompass diverse transcription factors, protein kinases, protein phosphatases, enzymes worried in phospholipid metabolism, and different signaling molecules inclusive of calmodulin-binding protein. Many transcription factor genes have been stress inducible, suggesting that numerous transcriptional regulatory mechanisms can also function in regulating heat, drought, cold, or excessive salinity stress signal transduction pathways. Those transcription factors could govern expression of stress-inducible genes both cooperatively and independently [16].
Many techniques have been carried out to evaluate the gene expression for the improvement of plants such as subtractive hybridization of cDNA (Deoxyribonucleic Acid) libraries, homology searching, differential display, genome-wide identification and third generation sequencing [17]. Differential display reverse transcriptase polymerase chain reaction (DDRT-PCR) is a delicate, easy and significant technique to evaluate cDNA [18]. Differential display has benefit as compare to other techniques because big quantity of RNA (Ribonucleic acid) is not needed for analysis. It has been used with great success to identify several differentially expressed genes from plants [19]. The main thing is to do research by using oligonucleotide primers, of which one will be used as anchored primer to the poly-adenylate tail of mRNAs subgroup and the second will be used as arbitrary that will be short in sequence length so that it may combine at different positions as compare to the first primers [20]. The resulted mRNA after using these primer can then be manipulate by using RT-PCR (Reverse transcription polymerase chain reaction) and checked on agarose gel. Multiple primer’s pairs can be used to obtain the complementary DNA fragments that depend on strong link with sequence specificity of respective primer. Novel HSP70 genes expressed under stressful conditions have been identified and isolated from tomato, Arabidopsis and wheat by using the DDPCR [21, 22, 23]. However, number of genes studied in one attempt of experiment are low as compared to the other advanced techniques like high-throughput expression profiling as qPCR (quantitative polymerase chain reaction) and Northern blotting [24, 25]. Advancements of second-generation sequencing technology offers opportunities for the discovery of millions of novel markers in non-model crop organisms as well as the detection of genes for agronomic traits [26]. Identification of genes within a population gives an understanding that how essential is to control the agronomic traits. The ability to produce sequence data is being supported by increasingly high throughput technologies such as next or second-generation sequencing. It identify the systems that yield vast number (usually millions) of short DNA sequence reads between 25 and 400 bp [27].
The first model plant genome sequenced was Arabidopsis thaliana (Arabidopsis Genome, 2000) and first crop genome sequenced was the Rice [28, 29, 30]. Current crop genome sequencing programmes are quickly shifting pace with emerging technology that’s why second-generation sequencing is adopted to obtain insight into their chosen genome. Although the sequencing and assembly of large and complex crop genomes remains an important task, a considerable amount of information can be obtained from low-coverage shotgun sequencing of these genomes. Short paired reading data generated using second generation technologies are especially suited for the discovery of genes and gene promoters in crop plants [31, 32]. Many HSP70 genes from different species such as Agave sisalana [10]; Solanum tuberosum [33, 34]; common bean [35]; A. thaliana [36]; Populus [37] have been described at transcription that expresses under heat stress. Four transcriptional regulatory systems have also been reported, two of them are ABA-independent (Abscisic acid) whereas other two are ABA-dependent. Genetic and molecular analyses suggested cross talk between these regulatory systems. Genomic analyses of stress-inducible genes have recently revealed cross talk in stress-responsive gene expression [33, 34, 38, 39].
4. HSP70 gene family leading to improve abiotic stress tolerance in plant
Plants accumulate specific stress responsive proteins under harsh environmental conditions [40]. Heat-shock proteins (HSPs) and late embryogenesis abundant (LEA) proteins accumulate under salinity, extreme temperature and water stress. These proteins have been shown to be involved in cellular protection during the stress [41, 42]. Enzymes and proteins are not able to function during abiotic stresses. Therefore, it is necessary for cell survival to prevent them from aggregation and maintain their functional conformations [3]. HSP70s are synthesized when environmental changes disturb an organism’s whole physiological system to such an extent that results in denaturation of proteins [43, 44]. Under such situation many stress associated proteins especially HSPs have been proven to act as molecular chaperones which play significant role in protein synthesis, maturation, degradation and targeting in an extensive array of ordinary mobile processes. Furthermore, molecular chaperones stabilize the proteins and membranes, in addition to assist in refolding of protein beneath stress conditions [45, 46]. They had been broadly documented in many plant species together with Arabidopsis, soybean, tobacco, rice, maize and wheat. They may be regularly expressed in plants constitutively but their expression is regulated by using various environmental conditions which include heat and salt [47]. Research have verified their presence in cytosol, mitochondria and chloroplast and play vital function in remodeling machines that participate in maintaining the integrity of the mobile proteome via facilitating protein reworking, disaggregation, reactivation or degradation of misfolded and inactive protein [13].
The cDNA coding HSP70 solubilizes and releases the aggregated protein in a kingdom that can be replenished with the assistance of small HSP gene circle of relatives as stated by way of Nillegoda et al., [48]. They’re generally cytoprotective, presenting thermo-tolerance that is specifically crucial for plant life [49]. The HSP70 superfamily’s genomic evaluation revealed an evolutionary history as phylogenetic tree of all HSP70 participants that cautioned the similarity of HSP70s in 12 subgroups, including the ones expressed formerly to the mammalian HSP110 and GRP170 in the identical sub-cell component. Growth in the expression of HSP70 in one of a kind plant species underneath heat stress situations has been studied appreciably by using proteomics and practical genomics [50]. A widespread osmoprotective effect changed into received in Escherichia coli transformed with the cytosolic chaperonin CCP-1a from Bruguiera sexangula [51].
HSPs have been studied extensively through plant transformation in response to heat stress [52]. Over expression of HSP101 from Arabidopsis in rice transgenic plants improved the growth performance after recovery from heat stress [53]. Heikkila et al. [54] demonstrated that exposure of seedlings of corn to ABA, water stress, heat shock, and wounding increases the synthesis of HSP70. Study of HSP70 in Rice, Tomato and Arabidopsis genomes revealed that about 37 genes of HSP70 were identified in rice, 30 in tomato 13 in Arabidopsis and 68 in A. sisalana and has been documented to be present within every cellular compartment of plants (Table 1).
The HSP70s have two huge functional domains, an ATPase domain within the N-terminal part of the protein and a peptide-binding domain within the C-terminal part of the protein [58]. The two domain names are more or less 40 & 25 kDa lengthy, respectively and are separated by means of a hinge location at risk of protease cleavage. Since the HSP70s are determined inside the cytosol, endoplasmic reticulum (ER), mitochondria and plastids, the N-terminal transit peptide of variable sequence is present in the precursor form of these individuals that make part for importation into the organelle [59]. For several HSP70s, a C-terminal subdomain of 5 kDa or much less is needed for plenty co-chaperone interactions (Figure 1) [36]. HSP70s exercising their role in several cell techniques by way of binding uncovered hydrophobic residues of non-native proteins during protein folding, stopping protein aggregation, selling the regeneration of combination proteins and keeping proteins in an import-able translocation surroundings to subcellular cubicles [9]. HSP70s interact in protein folding by means of chaperone strategies that encompass repeated cycles of peptide binding, ATP hydrolysis and peptide release. Cytosolic Hsp70s are lively in cellular strategies such as protein folding, denatured protein folding, protein aggregation prevention and protein retention in an import-capable eukaryotic surroundings [60]. There are some medical studies of plant cytosolic Hsp70s, but they are acknowledged to behave like different prokaryotic and eukaryotic HSP70s. In vitro experiments have proven that plant cytosolic Hsp70s mixes mysterious precursor polypeptides with nascent. Further, whilst wheat germ extract become removed from cytosolic Hsp70, co-translocation and processing of precursor proteins have become inefficient and the incorporation of cytosolic Hsp70 restored the translocation and processing of precursor proteins [61]. It is proposed that the cytoplasmic Hsp70s are involved within the ER-translocation precursor protein.
Figure 1.
Structure of HSP70: SBD (substrate binding domain), ATP (adenosine 5′-triphosphate), ADP (adenosine diphosphate).
Chloroplast Hsp70 homologs recognized to be energetic in import strategies are within the outer envelope membrane facing the cytoplasm and inter membrane space, the stroma and the thylacoid lumen. Hsp70 is concerned in early protein imports by using associating with chloroplast precursor proteins, based on move-linking and immune precipitation studies [62]. The precise characteristic of Hsp70 stays unclear, however it is proposed that precursor proteins are moved from the cytosolic HSP70s to the chloroplast HSP70s. This is confirmed through studies with Dnak as a model system and shows that HSP70s can join chloroplast precursor protein transit peptides [7]. Mitochondrial precursor protein translocation also occurs post-translationally and precursor proteins are once again preserved in an import-ready state with the useful resource of cytosolic HSP70s. Its homologs are positioned inside the outer mitochondrial membrane facing the cytosol and in the mitochondrial bean matrix [63]. An HSP70 homolog located in the outer membrane changed into suspected to be involved in protein translocation within the outer membrane with the aid of attaching the precursor proteins launched from the cytosolic Hsp70 and integrating them into the outer membrane. However, there may be no proof to guide this process. Matrix Hsp70, which has a strong homology to DnaK, is determined to be closely connected with the inner mitochondrial membrane of bean [36]. It is proposed that the HSP70 matrix may additionally result in internal membrane import by means of pulling precursor proteins into the matrix in an ATP-based method aided by using the GrpE mitochondrial co-chaperone homolog [64].
The ability of plants to tolerate dangerous effects of intense high temperature without irreversible harm is heat stress tolerance [65]. Effect of temperature contributes to a number of bad changes in plants’ life: extreme dehydration and dryness, chlorophyll burning and different physiological disorders. The cessation of protein synthesis improves the degradation and accumulation of ammonia poisonous substances [66]. However, the heat tolerance mechanisms in flora have been partly understood that HSP70 gene protect flowers from oxidative damage [67]. Additional mechanisms probably contributing to heat tolerance involve phytohormones, second messenger molecules which includes calcium (Ca++) and an expansion of transcription factors [68]. The various downstream tactics, safety towards oxidative damage and protein aggregation at some stage in heat stress are critical for preserving mobile membrane integrity and photosynthesis. Consequently, over-expression of HSP70s initially regarded to be a promising technique for engineering to evaluate the heat tolerance in vegetation; but, best restricted success has been reported in past many years [69], and no field tests, heat tolerant and transgenic line has been stated. These observations advocate that a single stress tolerance mechanism might not be sufficient and additional mechanisms will be had to generate durable heat-tolerant cultivars. Highly conserved protein, HSP70s are omnipresent proteins first-class acknowledged for their susceptibility to numerous stresses consisting of heat stress [70]. HSP70 assist to place every protein inside the organelles of the cellular and interplay the mitochondrion and chloroplast proteins [11]. They’ve a link to proteasomal degradation pathway mediated through ubiquitin. In addition unfolded outer membrane proteins in the intercellular spaces transduce a signal to the inner membrane proteins under hot temperature inside the cytosol. This causes the heat shock transcription factors to be activated [71]. These heat shock transcription factors (HSFs) associated with HSP70 are one of the maximum reported protein families. They commonly hold collectively with heaat shock induced factors (HSEs) within the promoter areas to set off their expression, which transcribes the HSP70 (Figure 2).
7. HSP70 confers the tolerance to heat stress in plants
As the primary pigment of plants, chlorophyll (Chl) plays a crucial role in the mechanism of photosynthesis and its contents. Role of HSP70 in the prevention of heat, stress, chlorophyll and water breakdown was determined in transgenic tobacco and cotton seedlings. As seen in research conducted by Batcho et al., [52] & Wang et al., [72], overall output of chl, chl (a) and chl (b) content of the non-transgenic plants were decreased with the extension of treatment time after treatment with heat stress. However, the total Chl, Chla and Chlb content of HSP70 transgenic plants was higher and the reduction was slower when compared to the controls. Assay of soluble sugar content and comparative electrical conductivity of transgenic plants was improved during heat treatment when compared to control plants. This suggests that the relative electrolyte leakage of the control plants was evidently higher and the damage to the cell membrane was severe. This is consistent with the studies of [36, 73] indicating that HSP70 is involved in response to heat stress in plants.
Overexpression of HSP70 was found to decrease the malondialdehyde (MDA) content and increased production of superoxide dismutase (SOD) and peroxidase (POD) in transgenic plants when compared to control [74]. Some reactive oxygen species (ROS) such as superoxide, hydrogen peroxide and hydroxyl radicals will be synthesized and accumulated when plants are heat stressed. These ROS are cytotoxic through inactivating enzymes and killing essential cellular components such as cell membranes by oxidative processes’ damage. MDA is the final product of peroxidation of the membrane. The higher the peroxidation, larger the amount of MDA produced. Plants have developed several defensive pathways to reduce oxidative damage and mitigate adverse effects. Transgenic tobacco plants demonstrated the higher overall activity of SOD and POD. This suggested that there would be less accumulation of ROS in transgenic and a better state of growth under heat stress. It has been found that overexpression of HSP70 increased the soluble sugar content and decreased the electrical conductivity in transgenic plants. The cell membrane also experiences primary physiological injuries which results the cell electrolyte leakage under heat stress [75].
Heat Shock Protein Gene70 (HSP70) is one of the solutions to induce heat stress tolerance in agriculturally important crop plants. These genes identified, isolated from local environment/habitat and local plant species will be helpful to make the genetic transformation of local varieties of desirable plants. The modern genomic approaches will be helpful for the characterization of genes at transcriptional or promoter level to modify the gene and to enhance the gene expression in transgenic crops. Hence the HSP70 will be a suitable target to combat the crops against global warming threat to crops.
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Written By
Fatima Batool, Batcho Anicet Agossa, Zainab Y. Sandhu, Muhammad Bilal Sarwar, Sameera Hassan and Bushra Rashid
Submitted: 12 April 2022Reviewed: 12 May 2022Published: 26 June 2022
Open access peer-reviewed chapter
