title: The first phytoplasma RNase P RNA provides new insights into the sequence requirements of this ribozyme.
abstract: A high variability of RNase P RNA structures is seen among members of the Mycoplasma group. To gain further insight into the structure-function relations of this ribozyme, we have searched for the RNase P RNA gene from more distant relatives, the phytoplasmas. These mycoplasma-like organisms are the aetiological agents of many severe plant diseases. We report the sequence and catalytic properties of RNase P RNA from the phytoplasma causing apple proliferation disease. The primary and postulated secondary structure of this 443 nt long RNA are most similar to those of Acholeplasma, supporting the phylogenetic position of this pathogen. Remarkably, the extremely AT-rich (73.6%) phytoplasma RNA differs from the known bacterial consensus sequence by a single base pair, which is positioned close to the substrate cleavage site in current three-dimensional models. Phytoplasma RNase P RNA functions as an efficient ribozyme in vitro. Conversion of its sequence to the full consensus and kinetic analysis of the resulting mutant RNAs suggests that neither the sequence alone, nor the type of pairing at this position is crucial for substrate binding or catalysis by the RNase P ribozyme. These results refine the bacterial consensus structure close to the catalytic core and thus improve our understanding of RNase P RNA function.
authors: Institut für Biochemie, Bayerische Julius-Maximilians-Universität, Biozentrum, Am Hubland, D-97074 Würzburg, Germany.
authors: M
authors: M
authors: Wagner
authors: C
authors: C
authors: Fingerhut
authors: H J
authors: HJ
authors: Gross
authors: A
authors: A
authors: Schön
mesh_terms: D000129:Acholeplasmataceae / Q000201:enzymology* / Q000235:genetics*; D020029:Base Pairing; D001483:Base Sequence; D001665:Binding Sites; D002384:Catalysis; D016384:Consensus Sequence / Q000235:genetics; D004722:Endoribonucleases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D009690:Nucleic Acid Conformation; D010802:Phylogeny; D010935:Plant Diseases / Q000382:microbiology; D012322:RNA Precursors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D020871:RNA Stability / Q000235:genetics; D016337:RNA, Catalytic / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D012365:RNA, Transfer, Tyr / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D043262:Ribonuclease P; D013329:Structure-Activity Relationship; D013816:Thermodynamics
chemical_list: D029968:Escherichia coli Proteins; D012322:RNA Precursors; D016337:RNA, Catalytic; D012365:RNA, Transfer, Tyr; D004722:Endoribonucleases; D043262:Ribonuclease P; C470865:ribonuclease P, E coli; D008274:Magnesium