Analysis of the tertiary structure of bacterial RNase P RNA.
The ubiquitous occurrence of ribonuclease P (RNase P) as a ribonucleoprotein and the catalytic properties of bacterial RNase P RNAs indicate that RNA fulfills an ancient and important role in the function of this enzyme. This review focuses on efforts to determine the structure of the bacterial RNase P RNA ribozyme. Phylogenetic comparative analysis of a library of bacterial RNase P RNA sequences has resulted in a well-developed secondary structure model and allowed identification of some elements of tertiary structure. The native structure has been redesigned by circular permutation to facilitate intra- and inter-molecular crosslinking experiments in order to gain further structural information. The crosslinking constraints, together with the constraints provided by comparative analyses, have been incorporated into a first-order model of the structure of of the ribozyme-substrate complex. The developing structural perspective allows the design of self-cleaving pre-tRNA-RNase P RNA conjugates which are useful tools for additional structure-probing experiments.
Harris
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Department of Biology, Indiana University, Bloomington 47402, USA.
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D001419:Bacteria / Q000201:enzymology*; D001483:Base Sequence; D004722:Endoribonucleases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010802:Phylogeny; D012322:RNA Precursors / Q000737:chemistry / Q000378:metabolism; D012329:RNA, Bacterial / Q000737:chemistry* / Q000378:metabolism; D016337:RNA, Catalytic / Q000737:chemistry* / Q000378:metabolism; D043262:Ribonuclease P; D012261:Ribonucleoproteins / Q000737:chemistry
D012322:RNA Precursors; D012329:RNA, Bacterial; D016337:RNA, Catalytic; D012261:Ribonucleoproteins; D004722:Endoribonucleases; D043262:Ribonuclease P