Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle
Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle
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DOI：
10.1006/jmbi.2000.4454
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发表时间：
2001-03-16
影响因子：
5.6
通讯作者：
Doudna, JA
中科院分区：
文献类型：
--
作者：
Batey, RT;Sagar, MB;Doudna, JA
信号识别颗粒（SRP）是一种核糖核蛋白复合物，负责将蛋白质靶向真核生物的内质网或原核生物的内膜。大肠杆菌 SRP 普遍保守的 RNA 蛋白核心的晶体结构，在此精炼至 1.5 埃分辨率，揭示了 Ffh 蛋白的 M 结构域对 4.5 S RNA 成分的小沟识别。在 RNA 内，包含两个系统发育保守内部环的核苷酸为蛋白质识别创建了独特的表面。为了确定保守核苷酸对于 SRP 组装的能量重要性，我们测量了 M 结构域对一系列 RNA 突变体的亲和力。该分析揭示了两个内部环基序内的保守核苷酸如何建立大分子界面的结构并定位必要的功能基团以供蛋白质直接识别。 (C) 2001 年学术出版社。
The signal recognition particle (SRP) is a ribonucleoprotein complex responsible for targeting proteins to the endoplasmic reticulum in eukarya or to the inner membrane in prokarya. The crystal structure of the universally conserved RNA-protein core of the Escherichia coli SRP, refined here to 1.5 Angstrom resolution, revealed minor groove recognition of the 4.5 S RNA component by the M domain of the Ffh protein. Within the RNA, nucleotides comprising two phylogenetically conserved internal loops create a unique surface for protein recognition. To determine the energetic importance of conserved nucleotides for SRP assembly, we measured the affinity of the M domain for a series of RNA mutants. This analysis reveals how conserved nucleotides within the two internal loop motifs establish the architecture of the macromolecular interface and position essential functional groups for direct recognition by the protein. (C) 2001 Academic Press.