Liu Yun, Liu Guobao, Li Ranhui, Zou Yongdong, Zheng Yizhi
Key Laboratory of Microorganism and Genetic Engineering of Shenzhen City, College of Life Science, Shenzhen University, Shenzhen 518060, China.
Sheng Wu Gong Cheng Xue Bao. 2010 May;26(5):569-75.
Late embryogenesis abundant (LEA) proteins are well associated with the desiccation tolerance in organisms. LEA proteins are categorized into at least seven groups by virtue of similarities in their deduced amino acid sequences. Most of the LEA proteins have the characteristics of high hydrophilicity and thermo-stability. The LEA proteins are in unstructured conformation in aqueous solution. However, they adopted amphiphilic alpha-helix structure during desiccation condition. LEA proteins are localized to the different organelles in the cells, i.e. cytoplasm, endoplasmic reticulum, mitochondria and nucleus. The multi-functional capacity of LEA proteins are suggested, as protein stabilization, protection of enzyme activity, membrane association and stabilization, antioxidant function, metal-ion binding or DNA protection, etc. Here, we review the structural and functional characteristics of LEA proteins to provide a reference platform to understand their protective mechanisms during the adaptive response to desiccation in organisms.
胚胎发育晚期丰富(LEA)蛋白与生物体的耐干燥性密切相关。根据推导的氨基酸序列相似性,LEA蛋白至少可分为七组。大多数LEA蛋白具有高亲水性和热稳定性的特征。LEA蛋白在水溶液中呈无结构构象。然而,在干燥条件下它们会形成两亲性α-螺旋结构。LEA蛋白定位于细胞中的不同细胞器,即细胞质、内质网、线粒体和细胞核。LEA蛋白具有多种功能,如蛋白质稳定、酶活性保护、膜结合与稳定、抗氧化功能、金属离子结合或DNA保护等。在此,我们综述LEA蛋白的结构和功能特性,以提供一个参考平台,用于理解它们在生物体对干燥的适应性反应过程中的保护机制。