The many faces of RNA-based RNase P, an RNA-world relic. Issue 12 (December 2021)

• Record Type: Journal Article
• Authors: Phan, Hong-Duc; Lai, Lien B.; Zahurancik, Walter J.; Gopalan, Venkat
• Is Part Of: Trends in biochemical sciences. Volume 46:Issue 12(2021)
• Page Start: 976
• Page End: 991
• Publication Date: 2021-12
• Subjects: ribozyme -- catalytic ribonucleoprotein -- tRNA processing -- protein-aided RNA catalysis; Biochemistry -- Periodicals; 572
• DOI: 10.1016/j.tibs.2021.07.005
• Languages: English
• ISSNs: 0968-0004

Abstract

Abstract : RNase P is an essential enzyme that catalyzes removal of the 5′ leader from precursor transfer RNAs. The ribonucleoprotein (RNP) form of RNase P is present in all domains of life and comprises a single catalytic RNA (ribozyme) and a variable number of protein cofactors. Recent cryo-electron microscopy structures of representative archaeal and eukaryotic (nuclear) RNase P holoenzymes bound to tRNA substrate/product provide high-resolution detail on subunit organization, topology, and substrate recognition in these large, multisubunit catalytic RNPs. These structures point to the challenges in understanding how proteins modulate the RNA functional repertoire and how the structure of an ancient RNA-based catalyst was reshaped during evolution by new macromolecular associations that were likely necessitated by functional/regulatory coupling. Highlights: RNase P, as a ribonucleoprotein or protein-only form, catalyzes removal of the 5′ leader from precursor transfer RNAs (tRNAs). Recent cryo-electron microscopy structures of archaeal and eukaryotic RNase P ribonucleoproteins, combined with an earlier crystal structure of bacterial RNase P, point to the enduring use of conserved structural elements for substrate recognition and cleavage. The architecture of the single RNA embraced by the interlocking layout of five to ten proteins in archaeal and eukaryotic RNase P confirms earlier predictions from biochemical studies regarding the division of labor among multiple proteins in aiding RNA catalysis. The solvent-exposed surfaces evident in the archaeal and eukaryotic RNase P structures (with and without tRNA) provide clues to how their assemblies may be adapted for functional coupling in cellular interactomes.