Disorder and function: a review of the dehydrin protein family.

Disorder and function: a review of the dehydrin protein family.
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DOI:
10.3389/fpls.2014.00576
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发表时间:
2014
影响因子:
5.6
通讯作者:
Boddington KF
Boddington KF
中科院分区:
生物学2区
文献类型:
--
作者:
Graether SP;Boddington KF

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脱水蛋白是晚期胚胎发生丰富(LEA)蛋白家族的第二组成员。脱水蛋白的蛋白质结构可以通过存在三种保守的序列基序来描述,这三种基序被命名为K-、Y-和S-片段。根据定义,脱水蛋白必须至少含有一份富含赖氨酸的K-片段。干旱、寒冷和盐度等非生物胁迫会导致脱水蛋白基因和蛋白水平的上调。尽管有大量的遗传和蛋白质证据表明这些蛋白质在应激反应中的重要性,但体内的保护机制并不完全清楚。来自生化分析和定位实验的体外实验证据表明,脱水蛋白具有多种作用,包括膜保护、酶的低温保护和保护活性氧物种。脱水蛋白与膜的结合很可能是作为一种外周膜蛋白,因为蛋白质序列高度亲水,含有许多带电氨基酸。正因为如此,溶液中的脱水蛋白本质上是无序的蛋白质,也就是说,它们没有明确的二级或三级结构。尽管脱水蛋白无序,但研究表明,当它们与膜等配体结合时,会获得结构,当与离子结合时,可能会改变它们的低聚状态。我们回顾了目前已知的脱水蛋白序列及其结构,并检查了已被证明与这一蛋白质家族结合的各种配体。
Dehydration proteins (dehydrins) are group 2 members of the late embryogenesis abundant (LEA) protein family. The protein architecture of dehydrins can be described by the presence of three types of conserved sequence motifs that have been named the K-, Y-, and S-segments. By definition, a dehydrin must contain at least one copy of the lysine-rich K-segment. Abiotic stresses such as drought, cold, and salinity cause the upregulation of dehydrin mRNA and protein levels. Despite the large body of genetic and protein evidence of the importance of these proteins in stress response, the in vivo protective mechanism is not fully known. In vitro experimental evidence from biochemical assays and localization experiments suggests multiple roles for dehydrins, including membrane protection, cryoprotection of enzymes, and protection from reactive oxygen species. Membrane binding by dehydrins is likely to be as a peripheral membrane protein, since the protein sequences are highly hydrophilic and contain many charged amino acids. Because of this, dehydrins in solution are intrinsically disordered proteins, that is, they have no well-defined secondary or tertiary structure. Despite their disorder, dehydrins have been shown to gain structure when bound to ligands such as membranes, and to possibly change their oligomeric state when bound to ions. We review what is currently known about dehydrin sequences and their structures, and examine the various ligands that have been shown to bind to this family of proteins.
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