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Modular Architecture of Bacterial RNase P Ribozymes as a Structural Platform for RNA Nanostructure Design
Yuri Nozawa1, Megumi Hagihara1, Shigeyoshi Matsumura1
1Department of Chemistry Graduate School of Science and Engineering University of Toyama Gofuku 3190, Toyama, Japan.
Abstract:
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.
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