Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner.
Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner.
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DOI：
10.1021/bi8015982
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发表时间：
2008-11-11
期刊：
影响因子：
2.9
通讯作者：
Foster, Mark
中科院分区：
文献类型：
--
作者：
Amero, Carlos D.;Boomershine, William P.;Xu, Yiren;Foster, Mark
RNase P是一种普遍存在的核糖核蛋白金属酶，负责在前体trna成熟过程中切割其5 ' -leader序列。虽然RNA亚基本身在高单价和二价离子浓度下具有催化活性，但在体内有四个蛋白质亚基与古细菌RNase P活性相关：RPP21、RPP29、RPP30和POP5。这些蛋白已被证明成对发挥作用：RPP21-RPP29和POP5-RPP30。我们利用常规和顺磁核磁共振技术测定了超嗜热古细菌furiosus （Pfu）中RPP21的溶液结构。溶液中的Pfu RPP21由一个非结构化的n端、两个α螺旋、一个锌结合基序和一个非结构化的c端组成。此外，我们还使用化学位移扰动来表征RPP21与Pfu RPP29的相互作用。数据表明，与RPP29的主要接触定位在RPP21的两个螺旋上。这些信息代表了理解古细菌RNase P全酶结构-功能关系的基本步骤。
RNase P is the ubiquitous ribonucleoprotein metalloenzyme responsible for cleaving the 5′-leader sequence of precursor tRNAs during their maturation. While the RNA subunit is catalytically active on its own at high monovalent and divalent ion concentration, four proteins subunits are associated with archaeal RNase P activity in vivo: RPP21, RPP29, RPP30 and POP5. These proteins have been shown to function in pairs: RPP21-RPP29 and POP5-RPP30. We have determined the solution structure of RPP21 from the hyperthermophilic archaeon Pyrococcus furiosus (Pfu) using conventional and paramagnetic NMR techniques. Pfu RPP21 in solution consists of an unstructured N-terminus, two alpha helices, a zinc binding motif, and an unstructured C-terminus. Moreover, we have used chemical shift perturbations to characterize the interaction of RPP21 with Pfu RPP29. The data show that the primary contact with RPP29 is localized to the two helices of RPP21. This information represents a fundamental step towards understanding structure-function relationships of the archaeal RNase P holoenzyme.
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