The specificity landscape of bacterial ribonuclease P

Chamberlain, Alexandra R.; Huynh, Loc; Huang, Wei; Taylor, Derek J.; Harris, Michael E.

doi:10.1016/j.jbc.2023.105498

Cited by 3 publications

(1 citation statement)

References 117 publications

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“…Thus, the bacterial RNase P is a dynamic enzyme that forms an initial encounter complex (enzyme–substrate/ES) upon recognition of a pre‐tRNA substrate, organizes the transition to the activated catalytic conformation (ES*) by unwinding extended acceptor stem pairings, if present, and employs a combination of stacking interactions and shape complementarity to elicit cleavage (Zhu et al, 2022). The bacterial RNP RNase P is further reviewed in other excellent articles (Chamberlain et al, 2023; Gößringer et al, 2021; Mohanty & Kushner, 2019; Mondragon, 2013; Phan et al, 2021; Schencking et al, 2020; Shaukat et al, 2021).…”

Section: Ribonucleoprotein Rnase P (Rnp Rnase P)mentioning

confidence: 99%

Multiple structural flavors of RNase P in precursor tRNA processing

Sridhara

2024

WIREs RNA

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The precursor transfer RNAs (pre‐tRNAs) require extensive processing to generate mature tRNAs possessing proper fold, structural stability, and functionality required to sustain cellular viability. The road to tRNA maturation follows an ordered process: 5′‐processing, 3′‐processing, modifications at specific sites, if any, and 3′‐CCA addition before aminoacylation and recruitment to the cellular protein synthesis machinery. Ribonuclease P (RNase P) is a universally conserved endonuclease in all domains of life, performing the hydrolysis of pre‐tRNA sequences at the 5′ end by the removal of phosphodiester linkages between nucleotides at position −1 and +1. Except for an archaeal species: Nanoarchaeum equitans where tRNAs are transcribed from leaderless‐position +1, RNase P is indispensable for life and displays fundamental variations in terms of enzyme subunit composition, mechanism of substrate recognition and active site architecture, utilizing in all cases a two metal ion‐mediated conserved catalytic reaction. While the canonical RNA‐based ribonucleoprotein RNase P has been well‐known to occur in bacteria, archaea, and eukaryotes, the occurrence of RNA‐free protein‐only RNase P in eukaryotes and RNA‐free homologs of Aquifex RNase P in prokaryotes has been discovered more recently. This review aims to provide a comprehensive overview of structural diversity displayed by various RNA‐based and RNA‐free RNase P holoenzymes towards harnessing critical RNA–protein and protein–protein interactions in achieving conserved pre‐tRNA processing functionality. Furthermore, alternate roles and functional interchangeability of RNase P are discussed in the context of its employability in several clinical and biotechnological applications.This article is categorized under: RNA Processing > tRNA Processing RNA Evolution and Genomics > RNA and Ribonucleoprotein Evolution RNA Interactions with Proteins and Other Molecules > RNA‐Protein Complexes

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Section: Ribonucleoprotein Rnase P (Rnp Rnase P)mentioning

confidence: 99%

Multiple structural flavors of RNase P in precursor tRNA processing

Sridhara

2024

WIREs RNA

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A tribute to Sidney Altman, one of the architects of modern RNA biology

Gopalan,

Kirsebom

2024

Journal of Biological Chemistry

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Engineering of RNase P Ribozymes for Therapy against Human Cytomegalovirus Infection

Smith,

Zhang,

Trang

et al. 2024

Viruses

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Nucleic acid-based gene interference and editing strategies, such as antisense oligonucleotides, ribozymes, RNA interference (RNAi), and CRISPR/Cas9 coupled with guide RNAs, are exciting research tools and show great promise for clinical applications in treating various illnesses. RNase P ribozymes have been engineered for therapeutic applications against human viruses such as human cytomegalovirus (HCMV). M1 ribozyme, the catalytic RNA subunit of RNase P from Escherichia coli, can be converted into a sequence-specific endonuclease, M1GS ribozyme, which is capable of hydrolyzing an mRNA target base-pairing with the guide sequence. M1GS RNAs have been shown to hydrolyze essential HCMV mRNAs and block viral progeny production in virus-infected cell cultures. Furthermore, RNase P ribozyme variants with enhanced hydrolyzing activity can be generated by employing in vitro selection procedures and exhibit better ability in suppressing HCMV gene expression and replication in cultured cells. Additional studies have also examined the antiviral activity of RNase P ribozymes in mice in vivo. Using cytomegalovirus infection as an example, this review summarizes the principles underlying RNase P ribozyme-mediated gene inactivation, presents recent progress in engineering RNase P ribozymes for applications in vitro and in mice, and discusses the prospects of using M1GS technology for therapeutic applications against HCMV as well as other pathogenic viruses.

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The specificity landscape of bacterial ribonuclease P

Cited by 3 publications

References 117 publications

Multiple structural flavors of RNase P in precursor tRNA processing

Multiple structural flavors of RNase P in precursor tRNA processing

A tribute to Sidney Altman, one of the architects of modern RNA biology

Engineering of RNase P Ribozymes for Therapy against Human Cytomegalovirus Infection

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