Characterization of the Borrelia burgdorferi RNase P RNA gene reveals a novel tertiary interaction.
Characterization of the RNase P RNA gene derived from Borrelia burgdorferi reveals covariation of the conserved nucleotides at positions corresponding to nucleotides 128 and 230 in Escherichia coli RNase P RNA (M1 RNA). Single base substitutions at either of these positions in M1 RNA resulted in a lack of complementation of the temperature-sensitive phenotype associated with rnpA49 in vivo whereas complementation was observed for the double mutant M1 RNA or wild-type M1 RNA. Our in vitro data showed that M1 RNA harbouring a substitution at 128 or 230 cleaved a tRNA precursor both in the absence and presence of C5 with reduced efficiency compared to the wild-type and the double mutant M1 RNA. We conclude that the nucleotides at positions 128 and 230 establish a long-range tertiary interaction in RNase P RNA. Our data also suggest that this interaction together with the identity of the nucleotide at position 230 is important for Pb2+ induced cleavage at specific positions in M1 RNA.
Mattsson
J G
JG
National Veterinary Institute, Uppsala, Sweden.
Svärd
S G
SG
Kirsebom
L A
LA
D001483:Base Sequence; D015748:Borrelia burgdorferi Group / Q000235:genetics*; D003001:Cloning, Molecular; D004722:Endoribonucleases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial / Q000235:genetics*; D007854:Lead / Q000494:pharmacology; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D009942:Organometallic Compounds / Q000494:pharmacology; D017354:Point Mutation / Q000502:physiology; D012329:RNA, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016337:RNA, Catalytic / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012365:RNA, Transfer, Tyr / Q000378:metabolism; D043262:Ribonuclease P
D029968:Escherichia coli Proteins; D009942:Organometallic Compounds; D012329:RNA, Bacterial; D016337:RNA, Catalytic; D012365:RNA, Transfer, Tyr; D007854:Lead; D004722:Endoribonucleases; D043262:Ribonuclease P; C470865:ribonuclease P, E coli; C008261:lead acetate