Ribonuclease P pp 113-134 | Cite as

Roles of Metal Ions in RNase P Catalysis

Part of the Protein Reviews book series (PRON, volume 10)


As for other RNA, RNase P with its catalytic RNA subunit requires metal(II)-ions for function. Approximately 100 metal(II)-ions bind to the 400 residues long RNA and several to the precursor substrate, e.g., roughly 25–30 to a tRNA precursor substrate. To understand the function and the reaction catalyzed by RNase P an important task is to identify and characterize metal(II)-ions or metal binding sites that contribute to folding of the RNAs, interaction with the protein subunit(s), substrate binding and chemistry of cleavage. Over the years, different methods have been explored to extract information about how, were and when metal(II)-ions bind to RNA. In this chapter, I will discuss our current understanding of RNase P and metal(II)-ions and how this knowledge can be utilized to search for new candidate drugs referred to as metal mimics.


Cleavage Site Nucleophilic Attack Interaction Influence Scissile Bond Mediate Cleavage 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



I thank my colleagues over the years for a pleasant and stimulating working atmosphere, Dr. S. Dasgupta for comments on the manuscript, and Drs N.E. Mikkelsen and S. Trobro for help with the figures 1, 2 and 3. This work was supported by the Strategic Research Foundation, and the Swedish Research Council.


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Authors and Affiliations

  1. 1.Department of Cell and Molecular BiologyBiomedical Center, Uppsala UniversityUppsalaSweden

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