Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis.
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.
Smith
J Kristin
JK
Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109, USA.
Hsieh
John
J
Fierke
Carol A
CA
D001426:Bacterial Proteins / Q000737:chemistry*; D002384:Catalysis; D020134:Catalytic Domain; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D012329:RNA, Bacterial / Q000737:chemistry*; D043262:Ribonuclease P / Q000737:chemistry*
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D043262:Ribonuclease P