Reddy R, Shimba S
Department of Pharmacology, Baylor College of Medicine, Houston, TX 77030, USA.
Mol Biol Rep. 1995;22(2-3):81-5. doi: 10.1007/BF00988710.
RNase P, the enzyme response for 5'-end processing of tRNAs and 4.5S RNA, has been extensively characterized from E. coli. The RNA component of E. coli RNase P, without the protein, has the enzymatic activity and is the first true RNA enzyme to be characterized. RNase P and MRP are two distinct nuclear ribonucleoprotein (RNP) particles characterized in many eukaryotic cells including human, yeast and plant cells. There are many similarities between RNase P and MRP. These include: (1) sequence specific endonuclease activity; (2) homology at the primary and secondary structure levels; and (3) common proteins in both the RNPs. It is likely that RNase P and MRP originated from a common ancestor.
核糖核酸酶P是一种负责tRNA和4.5S RNA 5'端加工的酶,已对其进行了广泛的大肠杆菌特性研究。大肠杆菌核糖核酸酶P的RNA组分在没有蛋白质的情况下具有酶活性,是首个被鉴定的真正的RNA酶。核糖核酸酶P和线粒体RNA加工酶(MRP)是在包括人类、酵母和植物细胞在内的许多真核细胞中鉴定出的两种不同的核糖核蛋白(RNP)颗粒。核糖核酸酶P和MRP之间有许多相似之处。这些相似之处包括:(1)序列特异性内切核酸酶活性;(2)一级和二级结构水平的同源性;(3)两种核糖核蛋白中的共同蛋白质。核糖核酸酶P和MRP可能起源于共同的祖先。