PMID:2266141
| Citation |
Surratt, CK, Carter, BJ, Payne, RC and Hecht, SM (1990) Metal ion and substrate structure dependence of the processing of tRNA precursors by RNase P and M1 RNA. J. Biol. Chem. 265:22513-9 |
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| Abstract |
A synthetic tRNA precursor analog containing the structural elements of Escherichia coli tRNA(Phe) was characterized as a substrate for E. coli ribonuclease P and for M1 RNA, the catalytic RNA subunit. Processing of the synthetic precursor exhibited a Mg2+ dependence quite similar to that of natural tRNA precursors such as E. coli tRNA(Tyr) precursor. It was found that Sr2+, Ca2+, and Ba2+ ions promoted processing of the dimeric precursor at Mg2+ concentrations otherwise insufficient to support processing; very similar behavior was noted for E. coli tRNA(Tyr). As noted previously for natural tRNA precursors, the absence of the 3'-terminal CA sequence in the synthetic precursor diminished the facility of processing of this substrate by RNase P and M1 RNA. A study of the Mg2+ dependence of processing of the synthetic tRNA dimeric substrate radiolabeled between C75 and A76 provided unequivocal evidence for an alteration in the actual site of processing by E. coli RNase P as a function of Mg2+ concentration. This property was subsequently demonstrated to obtain (Carter, B. J., Vold, B.S., and Hecht, S. M. (1990) J. Biol. Chem. 265, 7100-7103) for a mutant Bacillus subtilis tRNAHis precursor containing a potential A-C base pair at the end of the acceptor stem. |
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| Keywords |
Base Sequence; Cations, Divalent; Endoribonucleases/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Kinetics; Magnesium/pharmacology; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; RNA Precursors/genetics; RNA Precursors/metabolism; RNA Processing, Post-Transcriptional; RNA, Transfer/genetics; RNA, Transfer/metabolism; RNA, Transfer, Tyr/genetics; RNA, Transfer, Tyr/metabolism; Ribonuclease P |
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