Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3

Makoto Kimura, Yoshimitsu Kakuta

Research output: Chapter in Book/Report/Conference proceedingChapter

6 Citations (Scopus)

Abstract

Pyrococcus horikoshii OT3 is a hyperthermophilic archaeaon -isolated from hydrothermal fluid. Because of their genetic features as well as hyperthermophilic properties, macromolecules produced by this thermophilic bacterium have served as an excellent model for structural biology. Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5′-leader sequence of precursor tRNA (pre-tRNA). We found that RNase P RNA (PhopRNA) and five proteins in P. horikoshii OT3 reconstituted RNase P activity that exhibited enzymatic properties like those of the authentic enzyme. A mutational analysis indicated that nucleotides A40, A41, and U44 in PhopRNA are crucial for catalysis, strongly suggesting that PhopRNA catalyzes the hydrolysis of pre-tRNA in approximately the same manner as eubacterial RNase P RNAs, even though it has no enzymatic activity in the absence of the proteins. The P. horikoshii RNase P proteins are predominantly involved in optimization of PhopRNA's conformation, though individually they are dispensable for RNase P activity in vitro. This chapter summarizes structure-function relationships of the P. horikoshii RNase P subunits, including the high-resolution structural information that is currently available for the protein subunits.

Original languageEnglish
Title of host publicationMicroorganisms in Sustainable Agriculture and Biotechnology
PublisherSpringer Netherlands
Pages487-508
Number of pages22
Volume9789400722149
ISBN (Electronic)9789400722149
ISBN (Print)9400722133, 9789400722132
DOIs
Publication statusPublished - Oct 1 2012

All Science Journal Classification (ASJC) codes

  • Immunology and Microbiology(all)

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