title: RNase P RNA structure and cleavage reflect the primary structure of tRNA genes.
abstract: The function of RNase P RNA depends on its folding in space. A majority of RNase P RNAs from various bacteria show a similar secondary structure to that of Escherichia coli (M1 RNA). However, there are exceptions as exemplified by the RNase P RNA derived from the low GC-content Gram-positive bacteria Bacillus subtilis and Mycoplasma hyopneumoniae (Hyo P RNA). Previous studies using M1 RNA and Hyo P RNA suggest differences both with respect to the kinetics of cleavage as well as to cleavage site recognition. Here we have studied cleavage by these two structurally different RNase P RNAs as a function of changes in the 5' leader and the 3'-terminal CCA motif in the substrate. Our data suggest that the nucleotide at the -2 position in the 5' leader plays a role both for cleavage site recognition and for the rate of cleavage. However, depending on the identity of the -2 residue differences in the cleavage pattern comparing these two types of RNase P RNAs were observed. The results also suggest that the identity of the -1/+73 base-pair in the substrate influences the cleavage site recognition process. These findings will be related to differences in structure comparing these types of RNase P RNAs and the "RCCA-RNase P RNA" interaction. In addition, our findings will be discussed with respect to the primary structure of the tRNA genes in different bacteria.
authors.affiliation: Biomedical Centre, Uppsala, SE-751 23, Sweden.
authors.forename: M
authors.initials: M
authors.lastname: Brännvall
authors.forename: J G
authors.initials: JG
authors.lastname: Mattsson
authors.forename: S G
authors.initials: SG
authors.lastname: Svärd
authors.forename: L A
authors.initials: LA
authors.lastname: Kirsebom
mesh_terms: D001483:Base Sequence; D004722:Endoribonucleases / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins; D007700:Kinetics; D008969:Molecular Sequence Data; D009174:Mycoplasma / Q000201:enzymology; D009690:Nucleic Acid Conformation; D012313:RNA / Q000737:chemistry*; D012329:RNA, Bacterial / Q000737:chemistry; D016337:RNA, Catalytic / Q000737:chemistry*; D012343:RNA, Transfer / Q000235:genetics*; D043262:Ribonuclease P; D013379:Substrate Specificity
chemical_list: D029968:Escherichia coli Proteins; D012329:RNA, Bacterial; D016337:RNA, Catalytic; D012313:RNA; D012343:RNA, Transfer; D004722:Endoribonucleases; D043262:Ribonuclease P; C470865:ribonuclease P, E coli