Recent insights into the structure and function of the ribonucleoprotein enzyme ribonuclease P.
In bacteria, the tRNA-processing endonuclease ribonuclease P is composed of a large ( approximately 400 nucleotide) catalytic RNA and a smaller ( approximately 100 amino acid) protein subunit that is essential for substrate recognition. Current biochemical and biophysical investigations are providing fresh insights into the modular architecture of the ribozyme, the mechanisms of substrate specificity and the role of essential metal ions in catalysis. Together with recent high-resolution structures of portions of the ribozyme, these findings are beginning to reveal how the functions of RNA and protein are coordinated in this ribonucleoprotein enzyme.
Harris
Michael E
ME
Center for RNA Molecular Biology, Case Western Reserve University, School of Medicine, 44106, Cleveland, OH 44106, USA. meh2@pop.cwru.edu
Christian
Eric L
EL
D001419:Bacteria / Q000201:enzymology / Q000378:metabolism*; D008670:Metals / Q000378:metabolism; D011487:Protein Conformation; D012343:RNA, Transfer / Q000378:metabolism*; D043262:Ribonuclease P / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity
D008670:Metals; D012343:RNA, Transfer; D043262:Ribonuclease P