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Ribonucleoprotein Ribonucleases P and MRP

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Ribonucleases

Part of the book series: Nucleic Acids and Molecular Biology ((NUCLEIC))

Abstract

Ribonucleoprotein Ribonuclease (RNase) P and RNase MRP consist of a large RNA component and an essential protein part. RNases P/MRP differ from all other known ribonucleases in that it is their RNA component, not protein that is responsible for the endonucleolytic cleavage of substrates. RNase P is universally essential in all three domains of life; the closely related RNase MRP is a ubiquitous eukaryotic enzyme. RNase P is primarily responsible for the maturation of the 5′-ends of tRNA, whereas RNase MRP is known to be involved in the maturation of eukaryotic rRNA and the degradation of specific mRNAs. Here we discuss available information on functions, structural organization, and mechanisms of substrate recognition and catalysis of RNases P/MRP.

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Acknowledgments

I apologize to the authors of works that were not cited in this brief review due to space limitations. I would like to thank Lydia Krasilnikova for her help with the manuscript preparation. This work was supported by NIH grant GM085149 to A.S.K.

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  1. Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA

    Andrey S. Krasilnikov

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  1. Temple University, 1900 North 12th Street, Philadelphia, PA 19122, USA

    Allen W. Nicholson

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Krasilnikov, A.S. (2011). Ribonucleoprotein Ribonucleases P and MRP. In: Nicholson, A. (eds) Ribonucleases. Nucleic Acids and Molecular Biology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-21078-5_13

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