Structural basis for activation of an archaeal ribonuclease P RNA by protein cofactors

Biosci Biotechnol Biochem. 2017 Sep;81(9):1670-1680. doi: 10.1080/09168451.2017.1353404. Epub 2017 Jul 17.

Abstract

Ribonuclease P (RNase P) is an endoribonuclease that catalyzes the processing of the 5'-leader sequence of precursor tRNA (pre-tRNA) in all phylogenetic domains. We have found that RNase P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 consists of RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38. Biochemical characterizations over the past 10 years have revealed that PhoPop5 and PhoRpp30 fold into a heterotetramer and cooperate to activate a catalytic domain (C-domain) in PhopRNA, whereas PhoRpp21 and PhoRpp29 form a heterodimer and function together to activate a specificity domain (S-domain) in PhopRNA. PhoRpp38 plays a role in elevation of the optimum temperature of RNase P activity, binding to kink-turn (K-turn) motifs in two stem-loops in PhopRNA. This review describes the structural and functional information on P. horikoshii RNase P, focusing on the structural basis for the PhopRNA activation by the five RNase P proteins.

Keywords: Pyrococcus horikoshii; Ribonuclease P; hyperthermophilic archaea; precursor tRNA processing; protein–RNA interactions.

Publication types

  • Review

MeSH terms

  • Archaeal Proteins / metabolism*
  • Base Sequence
  • Humans
  • Pyrococcus horikoshii / genetics*
  • Pyrococcus horikoshii / metabolism*
  • RNA, Archaeal / genetics
  • RNA, Archaeal / metabolism*
  • RNA, Transfer / metabolism*
  • Ribonuclease P / chemistry
  • Ribonuclease P / genetics*
  • Ribonuclease P / metabolism

Substances

  • Archaeal Proteins
  • RNA, Archaeal
  • RNA, Transfer
  • Ribonuclease P