Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14
Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14
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DOI：
10.1007/s12104-011-9297-2
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发表时间：
2011-10-01
影响因子：
0.9
通讯作者：
Perczel, Andras
中科院分区：
文献类型：
--
作者：
Agoston, Bianka Szalaine;Kovacs, Denes;Perczel, Andras
脱氢蛋白是一类胁迫蛋白，属于植物中的晚期胚胎发生丰富蛋白(LEA)家族，因其在种子形成后期高表达而得名。在体细胞中，它们的表达在正常情况下很低，但在水分胁迫、高盐度或寒冷引起的脱水时，它们的表达急剧增加。脱氢蛋白被认为是一种本质上无序的蛋白质，这对理解其结构与功能的关系是一个挑战。本文给出了长185个氨基酸的ERD14(对脱水14的早期反应)的骨架(1)H、(15)N和(13)CNMR归属，它是一种K(3)S式的典型的拟南芥脱水蛋白。二次化学位移和核磁共振弛豫数据表明，ERD14在接近自然条件下是完全无序的，运动受到一定限制，螺旋倾向为5-25%。这些结果表明，ERD14可能具有与其伴侣(S)功能相互作用的部分预制元件，为进一步在体外和体内进行详细的结构和功能研究奠定了基础。
Dehydrins are a class of stress proteins that belong to the family of Late Embryogenesis Abundant (LEA) proteins in plants, so named because they are highly expressed in late stages of seed formation. In somatic cells, their expression is very low under normal conditions, but increases critically upon dehydration elicited by water stress, high salinity or cold. Dehydrins are thought to be intrinsically disordered proteins, which represents a challenge in understanding their structure-function relationship. Herein we present the backbone (1)H, (15)N and (13)C NMR assignment of the 185 amino acid long ERD14 (Early Response to Dehydration 14), which is a K(3)S-type, typical dehydrin of A. thaliana. Secondary chemical shifts as well as NMR relaxation data show that ERD14 is fully disordered under near native conditions, with short regions of somewhat restricted motion and 5-25% helical propensity. These results suggest that ERD14 may have partially preformed elements for functional interaction with its partner(s) and set the stage for further detailed structural and functional studies of ERD14 both in vitro and in vivo.