Open AccessModular Architecture of Bacterial RNase P Ribozymes as a Structural Platform for RNA Nanostructure Design
Author(s) -
Yuri Nozawa,
Megumi Hagihara,
Shigeyoshi Matsumura,
Yoshiya Ikawa
Publication year - 2018
Publication title -
chimia
Language(s) - English
Resource type - Journals
eISSN - 2673-2424
pISSN - 0009-4293
DOI - 10.2533/chimia.2018.882
Subject(s) - ribozyme , ligase ribozyme , rnase p , rna , vs ribozyme , rnase h , ribonuclease , rnase mrp , mammalian cpeb3 ribozyme , non coding rna , computational biology , enzyme , biology , chemistry , biochemistry , gene
Ribonuclease P (RNase P) is a class of enzymes involved in the processing of precursor tRNAs to remove their 5'-leader sequences. Ribonuclease P enzymes are classified into two completely distinct classes, i.e. an RNA-based enzyme and a protein-only enzyme. The RNA-based enzyme functions as a ribozyme in which the catalytic machinery is supported by its RNA component consisting of a single RNA molecule. Bacterial RNase P RNAs are a classical class of ribozymes and their structures and catalytic mechanisms have been studied extensively. The bacterial RNase P ribozyme has a modular tertiary structure consisting of two large domains, each of which can self-fold without the partner domain. Such modular architecture, identification of which provided important insight into the function of this ribozyme, is attractive as a structural platform to design functional RNA nanostructures. The first section of this article briefly summarizes the diversity of RNase P mainly focusing on RNA-based enzymes. The second section describes the structures of bacterial RNase P ribozymes from the viewpoint of their application as modular tools in RNA nanostructure design. The last section summarizes the current state and next steps in modular engineering of RNase P RNAs, including possible design of RNase P ribozyme-based nanostructures.