The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.
The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.
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DOI：
10.3390/biom6020027
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发表时间：
2016-05-13
期刊：
影响因子：
5.5
通讯作者：
Fierke CA
中科院分区：
文献类型：
--
作者：
Klemm BP;Wu N;Chen Y;Liu X;Kaitany KJ;Howard MJ;Fierke CA
核糖核酸酶P（Ribonuclease P，RNase P）是一种重要的核酸内切酶，负责催化前体转移RNA的5'端成熟。自20世纪70年代发现以来，RNase P酶已在生命的三个领域中被鉴定和研究。有趣的是，RNase P要么是基于RNA的，具有催化RNA亚基，要么是具有差异进化分布的蛋白质（PRORP）酶。现有的结构数据，包括活性位点数据，提供了对催化和底物识别的深入了解。两种形式的RNase P酶的水解和动力学机制是相似的，但基于RNA的酶和PRORP酶的独特特征与不同的进化起源是一致的。各种RNase P酶，除了它们在tRNA 5'成熟中的主要作用之外，还催化各种替代底物的切割，表明RNase P在体内功能的多样化。综述最后讨论了该领域的最新进展和有趣的研究方向。
Ribonuclease P (RNase P) is an essential endonuclease responsible for catalyzing 5’ end maturation in precursor transfer RNAs. Since its discovery in the 1970s, RNase P enzymes have been identified and studied throughout the three domains of life. Interestingly, RNase P is either RNA-based, with a catalytic RNA subunit, or a protein-only (PRORP) enzyme with differential evolutionary distribution. The available structural data, including the active site data, provides insight into catalysis and substrate recognition. The hydrolytic and kinetic mechanisms of the two forms of RNase P enzymes are similar, yet features unique to the RNA-based and PRORP enzymes are consistent with different evolutionary origins. The various RNase P enzymes, in addition to their primary role in tRNA 5’ maturation, catalyze cleavage of a variety of alternative substrates, indicating a diversification of RNase P function in vivo. The review concludes with a discussion of recent advances and interesting research directions in the field.