Structural and mechanistic basis of RNA processing by protein-only ribonuclease P enzymes

Trends Biochem Sci. 2022 Nov;47(11):965-977. doi: 10.1016/j.tibs.2022.05.006. Epub 2022 Jun 18.


Ribonuclease P (RNase P) enzymes are responsible for the 5' processing of tRNA precursors. In addition to the well-characterised ribozyme-based RNase P enzymes, an evolutionarily distinct group of protein-only RNase Ps exists. These proteinaceous RNase Ps (PRORPs) can be found in all three domains of life and can be divided into two structurally different types: eukaryotic and prokaryotic. Recent structural studies on members of both families reveal a surprising diversity of molecular architectures, but also highlight conceptual and mechanistic similarities. Here, we provide a comparison between the different types of PRORP enzymes and review how the combination of structural, biochemical, and biophysical studies has led to a molecular picture of protein-mediated tRNA processing.

Keywords: HARP; PRORP; RNA processing; RNase P; ribonuclease; tRNA.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis* / genetics
  • Humans
  • RNA Processing, Post-Transcriptional
  • RNA, Catalytic* / metabolism
  • RNA, Transfer / metabolism
  • Ribonuclease P / chemistry
  • Ribonuclease P / genetics
  • Ribonuclease P / metabolism


  • RNA, Catalytic
  • RNA, Transfer
  • Ribonuclease P