Crystal structure of the specificity domain of ribonuclease P

Andrey S. Krasilnikov, Xiaojing Yang, Tao Pan and Alfonso Mondragón ()
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Andrey S. Krasilnikov: Northwestern University
Xiaojing Yang: Northwestern University
Tao Pan: University of Chicago
Alfonso Mondragón: Northwestern University

Nature, 2003, vol. 421, issue 6924, 760-764

Abstract: 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.

Date: 2003
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DOI: 10.1038/nature01386

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