胚胎晚期富集蛋白与生物的干旱胁迫耐受性.pdf

生 物 工 程 学 报 Chin J Biotech 2010, May 25; 26(5): 569–575 journals.im.ac.cn Chinese Journal of Biotechnology ISSN 1000-3061 cjb@im.ac.cn ©2010 CJB, All rights reserved. 综 述 胚胎晚期富集蛋白与生物的干旱胁迫耐受性 刘昀，刘国宝，李冉辉，邹永东，郑易之 深圳大学生命科学学院 深圳市微生物基因工程重点实验室，深圳 518060 摘 要: 胚胎晚期富集蛋白 (Late embryogenesis abundant ，LEA) 是参与生物体抵抗干旱胁迫的一类重要蛋白。LEA 蛋 白可分为7 组。大多数LEA 蛋白具有亲水性及热稳定性。LEA 蛋白在水溶液中通常为无折叠状态，但脱水胁迫可诱导 其转变为 α-螺旋。近年来关于 LEA 蛋白的研究取得了较多进展。研究结果表明 LEA 蛋白可定位于细胞内的多种细胞 器中，且LEA 蛋白可能具有多重保护作用，如保护蛋白质及酶活性、或保护细胞的膜结构、或具有抗氧化作用、结合 离子或保护DNA 等。以下主要介绍了LEA 蛋白的功能、二级结构及保护作用机制。 关键词: 胚胎晚期富集蛋白，干旱胁迫，亚细胞定位，蛋白质二级结构，多重保护功能 Functions of late embryogenesis abundant proteins in desiccation-tolerance of organisms: a review Yun Liu, Guobao Liu, Ranhui Li, Yongdong Zou, and Yizhi Zheng Key Laboratory of Microorganism and Genetic Engineering of Shenzhen City, College of Life Science, Shenzhen University, Shenzhen 518060, China Abstract: 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 α-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 acti