Evans Donald, Marquez Steven M, Pace Norman R
Department of Molecular, Cellular and Developmental Biology, University of Colorado at Boulder, Campus Box 347, Boulder, CO 80309-0347, USA.
Trends Biochem Sci. 2006 Jun;31(6):333-41. doi: 10.1016/j.tibs.2006.04.007. Epub 2006 May 6.
Ribonuclease P (RNase P) is an endonuclease involved in processing tRNA. It contains both RNA and protein subunits and occurs in all three domains of life: namely, Archaea, Bacteria and Eukarya. The RNase P RNA subunits from bacteria and some archaea are catalytically active in vitro, whereas those from eukaryotes and most archaea require protein subunits for activity. RNase P has been characterized biochemically and genetically in several systems, and detailed structural information is emerging for both RNA and protein subunits from phylogenetically diverse organisms. In vitro reconstitution of activity is providing insight into the role of proteins in the RNase P holoenzyme. Together, these findings are beginning to impart an understanding of the coevolution of the RNA and protein worlds.
核糖核酸酶P(RNase P)是一种参与tRNA加工的内切核酸酶。它包含RNA和蛋白质亚基,存在于生命的所有三个域中,即古细菌、细菌和真核生物。来自细菌和一些古细菌的RNase P RNA亚基在体外具有催化活性,而来自真核生物和大多数古细菌的亚基则需要蛋白质亚基才能发挥活性。RNase P已在多个系统中进行了生物化学和遗传学表征,并且来自系统发育多样生物的RNA和蛋白质亚基的详细结构信息正在不断涌现。活性的体外重建正在深入了解蛋白质在RNase P全酶中的作用。这些发现共同开始让人们对RNA世界和蛋白质世界的共同进化有了一定的理解。