Heat Shock Proteins
Heat Shock Proteins
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DOI：
10.1002/9781119432401.ch9
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发表时间：
2020-02
期刊：
影响因子：
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通讯作者：
Annu Yadav;Jitender Singh;K. Ranjan;Pankaj Kumar;Shivani Khanna;Madhuri Gupta;Vinay Kumar;S. H. Wani;Anil Sirohi
中科院分区：
文献类型：
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作者：
Annu Yadav;Jitender Singh;K. Ranjan;Pankaj Kumar;Shivani Khanna;Madhuri Gupta;Vinay Kumar;S. H. Wani;Anil Sirohi
高温是影响植物生长、代谢和生产力的主要环境胁迫之一。HT应激通常导致蛋白质功能障碍。因此，维持蛋白质的功能构象并防止非天然蛋白质的聚集对于细胞在应激下的存活特别重要。植物已经进化出一系列适应逆境的机制，如诱导热休克蛋白（HSP）。根据分子量，HSP有各种类型，如HSP 100、HSP 90、HSP 70、HSP 60和小热休克蛋白（sHSP）。所有主要的热休克蛋白都具有改善蛋白质错误折叠和聚集引起的问题的相关功能。然而，每个主要的HSP家族都有独特的作用机制。一些促进错误折叠的蛋白质（Lon，泛素和各种泛素缀合酶）的降解，而另一些结合不同类型的折叠中间体并阻止它们聚集（HSP 70和HSP 60）并促进已经聚集的蛋白质的再活化（HSP 100）。它们负责蛋白质折叠、组装、易位、重建正常蛋白质构象，并且可以在应激条件下帮助蛋白质重折叠。
High temperature (HT) is one of the major environmental stresses that affect plant growth, metabolism, and productivity. HT stress usually causes protein dysfunction. Therefore, maintaining proteins in their functional conformations and preventing the aggregation of non‐native proteins are particularly important for cell survival under stress. Plants have evolved a wide array of mechanisms for adaption to stressful environments such as induction of heat shock proteins (HSPs). According to molecular weight HSPs are of various types such as HSP100, HSP90, HSP70, HSP60, and small heat shock proteins (sHSP). All of the major HSPs have related functions of ameliorating the problems caused by protein misfolding and aggregation. However, each major HSP family has a unique mechanism of action. Some promote the degradation of misfolded proteins (Lon, ubiquitin, and various ubiquitin‐conjugating enzymes), whereas others bind to different types of folding intermediates and prevent them from aggregating (HSP70 and HSP60) and promotes the reactivation (HSP100) of proteins that have already aggregated. These are responsible for protein folding, assembly, translocation, reestablishing normal protein conformation, and can assist in protein refolding under stress conditions.