Structural basis for pre-tRNA recognition and processing by the human tRNA splicing endonuclease complex

Nat Struct Mol Biol. 2023 Jun;30(6):824-833. doi: 10.1038/s41594-023-00991-z. Epub 2023 May 25.

Abstract

Throughout bacteria, archaea and eukarya, certain tRNA transcripts contain introns. Pre-tRNAs with introns require splicing to form the mature anticodon stem loop. In eukaryotes, tRNA splicing is initiated by the heterotetrameric tRNA splicing endonuclease (TSEN) complex. All TSEN subunits are essential, and mutations within the complex are associated with a family of neurodevelopmental disorders known as pontocerebellar hypoplasia (PCH). Here, we report cryo-electron microscopy structures of the human TSEN-pre-tRNA complex. These structures reveal the overall architecture of the complex and the extensive tRNA binding interfaces. The structures share homology with archaeal TSENs but contain additional features important for pre-tRNA recognition. The TSEN54 subunit functions as a pivotal scaffold for the pre-tRNA and the two endonuclease subunits. Finally, the TSEN structures enable visualization of the molecular environments of PCH-causing missense mutations, providing insight into the mechanism of pre-tRNA splicing and PCH.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural

MeSH terms

  • Archaea
  • Cryoelectron Microscopy
  • Endoribonucleases* / metabolism
  • Eukaryota / genetics
  • Humans
  • Introns
  • Nucleic Acid Conformation
  • RNA Precursors* / metabolism
  • RNA Splicing
  • RNA, Transfer / metabolism

Substances

  • RNA Precursors
  • splicing endonuclease
  • Endoribonucleases
  • RNA, Transfer