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TitleStructure and mechanistic features of the prokaryotic minimal RNase P.
Journal, issue, pagesElife, Vol. 10, Year 2021
Publish dateJun 28, 2021
AuthorsRebecca Feyh / Nadine B Waeber / Simone Prinz / Pietro Ivan Giammarinaro / Gert Bange / Georg Hochberg / Roland K Hartmann / Florian Altegoer /
PubMed AbstractEndonucleolytic removal of 5'-leader sequences from tRNA precursor transcripts (pre-tRNAs) by ribonuclease P (RNase P) is essential for protein synthesis. Beyond RNA-based RNase P enzymes, protein- ...Endonucleolytic removal of 5'-leader sequences from tRNA precursor transcripts (pre-tRNAs) by ribonuclease P (RNase P) is essential for protein synthesis. Beyond RNA-based RNase P enzymes, protein-only versions of the enzyme exert this function in various eukarya (there termed PRORPs) and in some bacteria ( and close relatives); both enzyme types belong to distinct subgroups of the PIN domain metallonuclease superfamily. Homologs of RNase P (HARPs) are also expressed in some other bacteria and many archaea, where they coexist with RNA-based RNase P and do not represent the main RNase P activity. Here, we solved the structure of the bacterial HARP from by cryo-electron microscopy, revealing a novel screw-like dodecameric assembly. Biochemical experiments demonstrate that oligomerization is required for RNase P activity of HARPs. We propose that the tRNA substrate binds to an extended spike-helix (SH) domain that protrudes from the screw-like assembly to position the 5'-end in close proximity to the active site of the neighboring dimer. The structure suggests that eukaryotic PRORPs and prokaryotic HARPs recognize the same structural elements of pre-tRNAs (tRNA elbow region and cleavage site). Our analysis thus delivers the structural and mechanistic basis for pre-tRNA processing by the prokaryotic HARP system.
External linksElife / PubMed:34180399 / PubMed Central
MethodsEM (single particle)
Resolution3.37 Å
Structure data

12878

7og5

EMDB-12878, PDB-7og5:
RNA-free Ribonuclease P from Halorhodospira halophila
Method: EM (single particle) / Resolution: 3.37 Å

Source
  • Halorhodospira halophila SL1 (bacteria)
  • halorhodospira halophila (strain dsm 244 / sl1) (bacteria)
KeywordsHYDROLASE / RNAseP / metallonuclease / HARP

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