The acceptor stem in pre-tRNAs determines the cleavage specificity of RNase P.
As the result of an unusual RNase P specificity, some special, mature tRNAs have acceptor stems with eight instead of the common seven base pairs. The data from numerous studies suggest that some features in the tRNA domain of pre-tRNAs are important for this behaviour. Here, we show that only five base pairs in the acceptor stem of bacterial histidine tRNAs are required to obtain the changed cleavage site in an unrelated eukaryotic serine tRNA.
Institute for General Microbiology, Christian-Albrechts-Universität, Kiel, FRG.
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D001482:Base Composition / Q000235:genetics; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D004252:DNA Mutational Analysis; D004722:Endoribonucleases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D029968:Escherichia coli Proteins; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012322:RNA Precursors / Q000378:metabolism*; D012329:RNA, Bacterial / Q000378:metabolism*; D016337:RNA, Catalytic / Q000378:metabolism*; D012354:RNA, Transfer, His / Q000378:metabolism*; D012362:RNA, Transfer, Ser / Q000378:metabolism*; D043262:Ribonuclease P
D029968:Escherichia coli Proteins; D012322:RNA Precursors; D012329:RNA, Bacterial; D016337:RNA, Catalytic; D012354:RNA, Transfer, His; D012362:RNA, Transfer, Ser; D004722:Endoribonucleases; D043262:Ribonuclease P; C470865:ribonuclease P, E coli