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Biopolymers. 2007 Dec 5-15;87(5-6):329-38.

Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis.

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  • 1Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109, USA.


Ribonuclease P (RNase P) is a ribonucleoprotein (RNP) complex that catalyzes the metal-dependent maturation of the 5' end of precursor tRNAs (pre-tRNAs) in all organisms. RNase P is comprised of a catalytic RNA (P RNA), and at least one essential protein (P protein). Although P RNA is the catalytic subunit of the enzyme and is active in the absence of P protein under high salt concentrations in vitro, the protein is still required for enzyme activity in vivo. Therefore, the function of the P protein and how it interacts with both P RNA and pre-tRNA have been the focus of much ongoing research. RNA-protein interactions in RNase P serve a number of critical roles in the RNP including stabilizing the structure, and enhancing the affinity for substrates and metal ions. This review examines the role of RNA-protein interactions in bacterial RNase P from both structural and mechanistic perspectives.

(c) 2007 Wiley Periodicals, Inc.

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