Premium
Importance of RNA‐protein interactions in bacterial ribonuclease P structure and catalysis
Author(s) -
Smith J. Kristin,
Hsieh John,
Fierke Carol A.
Publication year - 2007
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20846
Subject(s) - rnase p , rna , ribonucleoprotein , chemistry , ribonuclease , transfer rna , biochemistry , ribosome , riboswitch , non coding rna , gene
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. © 2007 Wiley Periodicals, Inc. Biopolymers 87: 329–338, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com