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The Heat-Shock Protein/Chaperone Network and Multiple Stress Resistance Pierre Jacob, Heribert Hirt, Abdelhafid Bendahmane

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The Heat-Shock Protein/Chaperone Network and Multiple Stress Resistance Pierre Jacob, Heribert Hirt, Abdelhafid Bendahmane The heat-shock protein/chaperone network and multiple stress resistance Pierre Jacob, Heribert Hirt, Abdelhafid Bendahmane To cite this version: Pierre Jacob, Heribert Hirt, Abdelhafid Bendahmane. The heat-shock protein/chaperone network and multiple stress resistance. Plant Biotechnology Journal, Wiley, 2017, 15 (4), pp.405-414. 10.1111/pbi.12659. hal-01602732 HAL Id: hal-01602732 https://hal.archives-ouvertes.fr/hal-01602732 Submitted on 27 May 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution| 4.0 International License Plant Biotechnology Journal (2017) 15, pp. 405–414 doi: 10.1111/pbi.12659 Review article The heat-shock protein/chaperone network and multiple stress resistance Pierre Jacob1, Heribert Hirt2,* and Abdelhafid Bendahmane1,* 1Institute of Plant Science—Paris-Saclay, Orsay, France 2Center for Desert Agriculture, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia Received 29 July 2016; Summary revised 25 October 2016; Crop yield has been greatly enhanced during the last century. However, most elite cultivars are accepted 3 November 2016. adapted to temperate climates and are not well suited to more stressful conditions. In the *Correspondence (Tel +331 69 15 33 30; context of climate change, stress resistance is a major concern. To overcome these difficulties, fax +331 69 15 34 24; email scientists may help breeders by providing genetic markers associated with stress resistance. [email protected], However, multistress resistance cannot be obtained from the simple addition of single stress Tel +96612 8082959; email [email protected]) resistance traits. In the field, stresses are unpredictable and several may occur at once. Consequently, the use of single stress resistance traits is often inadequate. Although it has been historically linked with the heat stress response, the heat-shock protein (HSP)/chaperone network is a major component of multiple stress responses. Among the HSP/chaperone ‘client proteins’, many are primary metabolism enzymes and signal transduction components with essential roles for the proper functioning of a cell. HSPs/chaperones are controlled by the action of diverse heat- shock factors, which are recruited under stress conditions. In this review, we give an overview of the regulation of the HSP/chaperone network with a focus on Arabidopsis thaliana. We illustrate Keywords: multistress resistance, the role of HSPs/chaperones in regulating diverse signalling pathways and discuss several basic stress acclimation, HSPs/chaperones, principles that should be considered for engineering multiple stress resistance in crops through HSF, crop improvement. the HSP/chaperone network. Introduction stress resistance. It is absolutely necessary to study multistress resistance pathways to understand and enhance canalization in Stresses are defined as environmental constraints that differ from the field (for review see Mittler and Blumwald (2010); Suzuki optimal conditions, ultimately impeding growth and develop- et al. (2014)). ment. As sessile organisms, plants are commonly exposed to One way to study multistress pathways would be to take fluctuating environments and can show a great degree of advantage of the pleiotropic HSP (heat-shock protein)/chaperone resilience to conditions that would be considered harmful to network. By definition, protein denaturation is a constant direct many other organisms. The process by which an organism or indirect consequence of any stress, as stresses are defined as reaches phenotypic stability despite environmental and genetic factors impeding normal cellular functions carried out by proteins. variations was termed ‘canalization’ (Waddington, 1961). Potentially, any stressor that induces protein misfolding would To improve canalization to extreme conditions, the selection of require HSP/chaperone recruitment. In this regard, chaperones stress resistance traits has been aided by the use of associated are now considered as powerful buffers against environmental genetic markers. Single stress resistance traits have been exten- stress and even genetic variations (Carey et al., 2006). Protein sively introgressed into elite cultivars. Due to the difficulty in misfolding is the main feature of heat stress, so the HSPs were the reproducing a specific stress of a specific strength, most genetic first chaperones to be studied. However, since the discovery of studies have remained limited to single stress resistance. In HSPs/chaperones, it has been found that the role of these factors nature, however, stresses rarely come alone. For instance, heat is not limited to heat stress management but is also involved in stress is associated with high light, but also facilitates the other stresses, such as cold, osmotic, drought, salt, UV, high light, spreading of pests and pathogens leading to dramatic production oxidative stress and pathogen infection (Swindell et al., 2007). losses. Moreover, responses to heat will involve the opening of Multistress resistance and the HSP/chaperone pathway stomata to dampen the rise in temperature, whereas a response to drought requires the closure of stomata to avoid water loss. In HSPs and chaperones are found in most prokaryotes and this regard, it is not surprising that responses to multiple, co- eukaryotes, and even some viruses (Maaroufi and Tanguay, occurring stresses are dramatically different than single stress 2013). In a cell, more than 10 000 proteins co-exist in a limited responses added together. Transcriptomic analyses lead to the space. Biochemists worldwide have experienced the difficulty in astonishing finding that 61% of the genes induced by dual producing only a few of these proteins in a native conformation in stresses were not induced by any of the single stresses concentrations comparable with in vivo conditions. Unfolded (Rasmussen et al., 2013). The combination of single stress proteins tend to form large aggregates that severely impede resistance traits will consequently mostly not lead to multiple normal cellular functions. The main function of HSPs/chaperones ª 2016 The Authors. Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd. 405 This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. 406 Pierre Jacob et al. is to act as a buffer to limit misfolding and resolve aggregates. By induced by HSFA3 overexpression (Yoshida et al., 2008). Simi- doing so, they minimize the impact of environmental and genetic larly, HSFA6a overexpression induces HSFA6b, HSFA5 and HSFA2 variations on the proteome. HSP90 alone makes up for 1%–2% (Hwang et al., 2014). Intriguingly, HSFA3 overexpression in of the total protein content in eukaryotes (Krukenberg et al., control conditions induces HSFA1e but not HSFA2 expression, 2011). The molecular mechanisms underlying the functions of which is induced by HSFA1e after heat and/or high light stress. HSPs have been extensively reviewed (Al-Whaibi, 2011; Fu, 2014; These complex interconnections and feedback loops demonstrate Niforou et al., 2014; Wang et al., 2013). Chaperone functions that multiple input signals can activate overlapping but different are not limited to folding and HSP70 and HSP90 and their HSF/HSP responses. cochaperones have clearly been linked to signalling, protein This adapted HSF activity may also be a consequence of post- targeting and degradation (Huang et al., 2014; Kadota and translational modifications (PTMs). HSFA4a is a target of MPK3 Shirasu, 2012; Kriechbaumer et al., 2012; Lee et al., 2009). and MPK6 (mitogen-activated protein kinase). It was reported that phosphorylation by MPK3/6 increases the activity of HSFA4a Transcriptional control of HSPs (Perez-Salam o et al., 2014). It was further shown that HSFA2 The basic principles of the transcriptional control of HSPs are phosphorylation by MPK6 is required for its nuclear localization, represented schematically in Figure 1. The main inducers of but the molecular mechanism determining the subcellular local- chaperones are heat-shock factors (HSF), grouped into three ization of HSFA2 has not been fully deciphered (Evrard et al., classes A, B and C (for review, see Guo et al. (2016); Nover et al. 2013). HSFA2 was also found to be sumoylated after heat stress (2001); Scharf et al. (2012)). HSFs are present in all eukaryotes, (Cohen-Peer et al., 2010) and an increased sumoylation was but plants show a large number of HSFs (38 in soya bean, 25 in correlated with a decrease in HSFA2 activity and diminished HSP rice, 21 in Arabidopsis) compared with a single HSF1 in induction. SUMO1-overexpressing plants showed an hsfa2 KO Saccharomyces cerevisiae or with seven members in humans phenotype with respect to heat stress tolerance. Most impor- (Fujimoto and Nakai, 2010). The diversity of the HSF family in tantly, it is thought that homo/hetero-oligomerization
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