期刊
BIOPOLYMERS
卷 87, 期 5-6, 页码 329-338出版社
WILEY
DOI: 10.1002/bip.20846
关键词
ribozyme; ribonucleoprotein; RNase P; review
资金
- NIGMS NIH HHS [T32 GM145304, R01 GM055387, GM 55387, T32 GM 08353, T32 GM008353] Funding Source: Medline
Ribonuelease 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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