生物
热休克蛋白
共同伴侣
蛋白质折叠
非生物胁迫
非生物成分
热休克蛋白70
蛋白质聚集
热休克蛋白90
折叠(DSP实现)
伴侣(临床)
细胞生物学
生物化学
生态学
基因
医学
工程类
病理
电气工程
作者
Wang‐Xia Wang,Basia Vinocur,Oded Shoseyov,Arie Altman
标识
DOI:10.1016/j.tplants.2004.03.006
摘要
Abstract
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 re-establishing 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 stress-induced components.
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