Xiao S, Houser-Scott F, Engelke D R
Department of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0606 USA.
J Cell Physiol. 2001 Apr;187(1):11-20. doi: 10.1002/1097-4652(200104)187:1<11::AID-JCP1055>3.0.CO;2-K.
Ribonuclease P is an ancient enzyme that cleaves pre-tRNAs to generate mature 5' ends. It contains an essential RNA subunit in Bacteria, Archaea, and Eukarya, but the degree to which the RNA subunit relies on proteins to supplement catalysis is highly variable. The eukaryotic nuclear holoenzyme has recently been found to contain almost twenty times the protein content of the bacterial enzymes, in addition to having split into at least two related enzymes with distinct substrate specificity. In this review, recent progress in understanding the molecular architecture and functions of nuclear forms of RNase P will be considered.
核糖核酸酶P是一种古老的酶，可切割前体tRNA以产生成熟的5'末端。在细菌、古细菌和真核生物中，它都包含一个必需的RNA亚基，但RNA亚基依赖蛋白质来补充催化作用的程度差异很大。最近发现，真核细胞核全酶除了已分裂为至少两种具有不同底物特异性的相关酶外，其蛋白质含量几乎是细菌酶的二十倍。在这篇综述中，我们将探讨在理解核糖核酸酶P核形式的分子结构和功能方面的最新进展。
