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- Title
Structural basis for activation of an archaeal ribonuclease P RNA by protein cofactors.
- Authors
Kimura, Makoto
- 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 archaeonPyrococcus horikoshiiOT3 consists of RNase P RNA (PhopRNA) and five protein cofactors designatedPhoPop5,PhoRpp21,PhoRpp29,PhoRpp30, andPhoRpp38. Biochemical characterizations over the past 10 years have revealed thatPhoPop5 andPhoRpp30 fold into a heterotetramer and cooperate to activate a catalytic domain (C-domain) inPhopRNA, whereasPhoRpp21 andPhoRpp29 form a heterodimer and function together to activate a specificity domain (S-domain) inPhopRNA.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 inPhopRNA. This review describes the structural and functional information onP. horikoshiiRNase P, focusing on the structural basis for thePhopRNA activation by the five RNase P proteins. A three-dimensional model ofPyrococcus horikoshiiRNase P in complex with tRNA on the basis of biochemical and structural data of theP. horikoshiiRNase P components.
- Subjects
RNA analysis; PHYLOGENETIC models
- Publication
Bioscience, Biotechnology & Biochemistry, 2017, Vol 81, Issue 9, p1670
- ISSN
0916-8451
- Publication type
Article
- DOI
10.1080/09168451.2017.1353404