A view of RNase P
- 25 July 2007
- journal article
- review article
- Published by Royal Society of Chemistry (RSC) in Molecular BioSystems
- Vol. 3 (9) , 604-607
- https://doi.org/10.1039/b707850c
Abstract
Major progress in the study of RNase P has resulted from crystallography of bacterial catalytic subunits and the discovery of catalytic activity in eukaryotes. Several new substrates have also been identified, primarily in bacteria but also in yeast. Our current world should be called the “RNA–protein world” rather than the “protein world”.Keywords
This publication has 32 references indexed in Scilit:
- RNase P: interface of the RNA and protein worldsTrends in Biochemical Sciences, 2006
- Structure of Pfu Pop5, an archaeal RNase P proteinProceedings of the National Academy of Sciences, 2006
- Crystal Structure of Protein Ph1481p in Complex with Protein Ph1877p of Archaeal RNase P from Pyrococcus horikoshii OT3: Implication of Dimer Formation of the HoloenzymeJournal of Molecular Biology, 2006
- Crystal structure of a bacterial ribonuclease P RNAProceedings of the National Academy of Sciences, 2005
- Crystal structure of the RNA component of bacterial ribonuclease PNature, 2005
- Crystal Structure of Archaeal Ribonuclease P Protein aRpp29 from Archaeoglobus fulgidus,Biochemistry, 2004
- Structure of Mth11/ Mth Rpp29, an essential protein subunit of archaeal and eukaryotic RNase PProceedings of the National Academy of Sciences, 2003
- Catalysis by RNase P RNAJournal of Biological Chemistry, 2003
- Molecular Modeling of the Three-dimensional Structure of the Bacterial RNase P HoloenzymeJournal of Molecular Biology, 2003
- Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysisJournal of Molecular Biology, 1998