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Crystal structure of the specificity domain of ribonuclease P

Author

Listed:
  • Andrey S. Krasilnikov

    (Northwestern University)

  • Xiaojing Yang

    (Northwestern University)

  • Tao Pan

    (University of Chicago)

  • Alfonso Mondragón

    (Northwestern University)

Abstract

RNase P is the only endonuclease responsible for processing the 5′ end of transfer RNA by cleaving a precursor and leading to tRNA maturation1,2. It contains an RNA component and a protein component and has been identified in all organisms. It was one of the first catalytic RNAs identified3 and the first that acts as a multiple-turnover enzyme in vivo. RNase P and the ribosome are so far the only two ribozymes known to be conserved in all kingdoms of life. The RNA component of bacterial RNase P can catalyse pre-tRNA cleavage in the absence of the RNase P protein in vitro and consists of two domains: a specificity domain and a catalytic domain4,5. Here we report a 3.15-Å resolution crystal structure of the 154-nucleotide specificity domain of Bacillus subtilis RNase P. The structure reveals the architecture of this domain, the interactions that maintain the overall fold of the molecule, a large non-helical but well-structured module that is conserved in all RNase P RNA, and the regions that are involved in interactions with the substrate.

Suggested Citation

  • Andrey S. Krasilnikov & Xiaojing Yang & Tao Pan & Alfonso Mondragón, 2003. "Crystal structure of the specificity domain of ribonuclease P," Nature, Nature, vol. 421(6924), pages 760-764, February.
    • Handle: RePEc:nat:nature:v:421:y:2003:i:6924:d:10.1038_nature01386
    DOI: 10.1038/nature01386
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