Life without RNase P

Nature. 2008 May 1;453(7191):120-3. doi: 10.1038/nature06833.

Abstract

The universality of ribonuclease P (RNase P), the ribonucleoprotein essential for transfer RNA (tRNA) 5' maturation, is challenged in the archaeon Nanoarchaeum equitans. Neither extensive computational analysis of the genome nor biochemical tests in cell extracts revealed the existence of this enzyme. Here we show that the conserved placement of its tRNA gene promoters allows the synthesis of leaderless tRNAs, whose presence was verified by the observation of 5' triphosphorylated mature tRNA species. Initiation of tRNA gene transcription requires a purine, which coincides with the finding that tRNAs with a cytosine in position 1 display unusually extended 5' termini with an extra purine residue. These tRNAs were shown to be substrates for their cognate aminoacyl-tRNA synthetases. These findings demonstrate how nature can cope with the loss of the universal and supposedly ancient RNase P through genomic rearrangement at tRNA genes under the pressure of genome condensation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acyl-tRNA Synthetases / metabolism
  • Aminoacylation
  • Base Sequence
  • Evolution, Molecular*
  • Gene Deletion
  • Genes, Archaeal / genetics*
  • Models, Biological
  • Molecular Sequence Data
  • Nanoarchaeota / cytology
  • Nanoarchaeota / enzymology
  • Nanoarchaeota / genetics*
  • Phosphorylation
  • Promoter Regions, Genetic / genetics*
  • RNA, Archaeal / genetics*
  • RNA, Archaeal / metabolism
  • RNA, Transfer / genetics*
  • RNA, Transfer / metabolism
  • Ribonuclease P / deficiency*
  • Ribonuclease P / metabolism
  • Substrate Specificity
  • Transcription, Genetic / genetics

Substances

  • RNA, Archaeal
  • RNA, Transfer
  • Ribonuclease P
  • Amino Acyl-tRNA Synthetases