Over a Decade of Bacterial Ribonuclease P Modeling
Ribonuclease P constitutes a unique paradigm for understanding RNA recognition, RNA catalysis as well as RNA–protein assembly. The modeling efforts, aiming at unraveling the architectural features of this ribozyme and the molecular basis conferring specificity in recognition of the pre-tRNA substrate and of the protein cofactor, are summarized in this chapter. The molecular models of the RNA subunits result from the integration of a great wealth of phylogenetic and biochemical data that have contributed to the understanding of the pre-tRNA recognition in the context of the two different A and B RNase P subtypes. Later efforts focused on the contribution of the protein subunit on both the binding to the RNA to form the holoenzyme and the selection of the substrate. The crystal structures of various components of the RNase P ribozyme show that the published 3D models successfully predicted the architectures of the RNase P RNAs. These crystal structures also show the need for further molecular modeling developments in order to improve the accuracy of the prediction and to apply them to the whole RNase P with its cofactor and substrate.
KeywordsLeader Sequence Comparative Sequence Analysis Folding Intermediate Tertiary Interaction Pace Model
- Kleywegt GJ, Jones TA (1994) A super position. CCP4/ESF-EACBM Newsletter Protein Crystallogr 31:9–14Google Scholar