期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 81, 期 9, 页码 1670-1680出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/09168451.2017.1353404
关键词
hyperthermophilic archaea; precursor tRNA processing; protein-RNA interactions; Pyrococcus horikoshii; Ribonuclease P
类别
资金
- National Project on Protein Structural and Functional Analyses from the Ministry of Education, Culture, Sports, Science, and Technology of Japan
- [15H04487]
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.
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