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比较植物冷激域蛋白、细菌和动物冷激域蛋白的结构、功能和调节。

Comparison of structure, function and regulation of plant cold shock domain proteins to bacterial and animal cold shock domain proteins.

机构信息

Division of Plant and Soil Sciences, West Virginia University, Morgantown, WV 26506-6108, USA.

出版信息

BMB Rep. 2010 Jan;43(1):1-8. doi: 10.5483/bmbrep.2010.43.1.001.

Abstract

The cold shock domain (CSD) is among the most ancient and well conserved nucleic acid binding domains from bacteria to higher animals and plants. The CSD facilitates binding to RNA, ssDNA and dsDNA and most functions attributed to cold shock domain proteins are mediated by this nucleic acid binding activity. In prokaryotes, cold shock domain proteins only contain a single CSD and are termed cold shock proteins (Csps). In animal model systems, various auxiliary domains are present in addition to the CSD and are commonly named Y-box proteins. Similar to animal CSPs, plant CSPs contain auxiliary C-terminal domains in addition to their N-terminal CSD. Cold shock domain proteins have been shown to play important roles in development and stress adaptation in wide variety of organisms. In this review, the structure, function and regulation of plant CSPs are compared and contrasted to the characteristics of bacterial and animal CSPs. [BMB reports 2010; 43(1): 1-8].

摘要

冷休克结构域(CSD)是从细菌到高等动物和植物中最古老和保存最完好的核酸结合结构域之一。CSD 有助于与 RNA、ssDNA 和 dsDNA 结合,并且归因于冷休克结构域蛋白的大多数功能都是通过这种核酸结合活性介导的。在原核生物中,冷休克结构域蛋白仅包含单个 CSD,称为冷休克蛋白(Csp)。在动物模型系统中,除了 CSD 之外,还存在各种辅助结构域,通常称为 Y 盒蛋白。与动物 CSP 类似,植物 CSP 除了其 N 端 CSD 外,还含有辅助的 C 端结构域。已经表明,冷休克结构域蛋白在广泛的生物体的发育和应激适应中发挥重要作用。在这篇综述中,将比较和对比植物 CSP 的结构、功能和调节与细菌和动物 CSP 的特征。[BMB 报告 2010;43(1): 1-8]。

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