In vitro hyperprocessing of tRNAs by Bacillus subtilis ribonuclease P RNA.
We have previously reported that the catalytic RNA subunit of ribonuclease P (RNase P) of Escherichia coli (M1 RNA) cleaves Drosophila initiator methionine tRNA (tRNA(i)Met), alanine tRNA (tRNA(Ala)) and histidine tRNA (tRNA(His)) within the mature tRNA sequences to produce specific fragments. We call this further cleavage hyperprocessing. These cleavages were dependent on the occurrence of altered conformations of the tRNAs. Here, we found that the RNase P RNA of Bacillus subtilis can hyperprocess these three tRNAs at the same sites as does M1 RNA. The hyperprocessing activity may probably be common feature for Bacterial RNase P RNAs.
Hori
Y
Y
Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku-cho, Toyohashi, Aichi 441-8580, Japan.
Tanaka
T
T
Kikuchi
Y
Y
D000818:Animals; D001412:Bacillus subtilis / Q000201:enzymology*; D001483:Base Sequence; D004330:Drosophila / Q000235:genetics; D004722:Endoribonucleases / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012323:RNA Processing, Post-Transcriptional; D012329:RNA, Bacterial / Q000378:metabolism*; D016337:RNA, Catalytic / Q000378:metabolism*; D012343:RNA, Transfer / Q000737:chemistry / Q000378:metabolism*; D043262:Ribonuclease P
D029968:Escherichia coli Proteins; D012329:RNA, Bacterial; D016337:RNA, Catalytic; D012343:RNA, Transfer; D004722:Endoribonucleases; D043262:Ribonuclease P; C470865:ribonuclease P, E coli