LEA proteins: IDPs with versatile functions in cellular dehydration tolerance

被引：160

作者：

Hincha, Dirk K. ^{[1
]}

Thalhammer, Anja ^{[1
]}

机构：

[1] Max Planck Inst Mol Pflanzenphysiol, D-14476 Potsdam, Germany

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2012年 / 40卷

关键词：

desiccation tolerance; enzyme stabilization; intrinsically disordered protein; late embryogenesis abundant protein (LEA protein); protein-membrane interaction; protein secondary structure; EMBRYOGENESIS-ABUNDANT PROTEIN; ARABIDOPSIS-THALIANA; SECONDARY STRUCTURE; FREEZING TOLERANCE; STRESS-PROTEINS; WATER-STRESS; COR15A GENE; MAIZE DHN1; DESICCATION; BINDING;

D O I：

10.1042/BST20120109

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

LEA (late embryogenesis abundant) proteins were originally described almost 30 years ago as accumulating late in plant seed development. They were later found to be induced in vegetative plant tissues under environmental stress conditions and also in desiccation-tolerant micro-organisms and invertebrates. Although they are widely assumed to play crucial roles in cellular dehydration tolerance, their physiological and biochemical functions are largely unknown. Most LEA proteins are predicted to be intrinsically disordered and this has been experimentally verified in several cases. In addition, some LEA proteins partially fold, mainly into a-helices, during drying or in the presence of membranes. Recent studies have concentrated on the potential roles of LEA proteins in stabilizing membranes or sensitive enzymes during freezing or drying, and the present review concentrates on these two possible functions of LEA proteins in cellular dehydration tolerance.

引用

页码：1000 / 1003

页数：4

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