Kazantsev Alexei V, Krivenko Angelika A, Harrington Daniel J, Carter Richard J, Holbrook Stephen R, Adams Paul D, Pace Norman R
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309-0347, USA.
Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7497-502. doi: 10.1073/pnas.0932597100. Epub 2003 Jun 10.
The structure of RNase P protein from the hyperthermophilic bacterium Thermotoga maritima was determined at 1.2-A resolution by using x-ray crystallography. This protein structure is from an ancestral-type RNase P and bears remarkable similarity to the recently determined structures of RNase P proteins from bacteria that have the distinct, Bacillus type of RNase P. These two types of protein span the extent of bacterial RNase P diversity, so the results generalize the structure of the bacterial RNase P protein. The broad phylogenetic conservation of structure and distribution of potential RNA-binding elements in the RNase P proteins indicate that all of these homologous proteins bind to their cognate RNAs primarily by interaction with the phylogenetically conserved core of the RNA. The protein is found to dimerize through an extensive, well-ordered interface. This dimerization may reflect a mechanism of thermal stability of the protein before assembly with the RNA moiety of the holoenzyme.
利用X射线晶体学技术，以1.2埃的分辨率测定了嗜热栖热菌（Thermotoga maritima）核糖核酸酶P（RNase P）蛋白的结构。该蛋白结构源自一种原始类型的RNase P，与最近测定的具有独特芽孢杆菌型RNase P的细菌的RNase P蛋白结构具有显著相似性。这两种类型的蛋白涵盖了细菌RNase P多样性的范围，因此这些结果概括了细菌RNase P蛋白的结构。RNase P蛋白中潜在RNA结合元件的结构和分布在广泛的系统发育中具有保守性，这表明所有这些同源蛋白主要通过与RNA的系统发育保守核心相互作用来结合其同源RNA。发现该蛋白通过一个广泛的、有序的界面形成二聚体。这种二聚化可能反映了该蛋白在与全酶的RNA部分组装之前的热稳定机制。
