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- W1985875854 abstract "RNase P with its catalytic RNA subunit is involved in the processing of a number of RNA precursors with different structures. However, precursor tRNAs are the most abundant substrates for RNase P. Available data suggest that a tRNA is folded into its characteristic structure already at the precursor state and that RNase P recognizes this structure. The tRNA D-/T-loop domain (TSL-region) is suggested to interact with the specificity domain of RNase P RNA while residues in the catalytic domain interact with the cleavage site. Here, we have studied the consequences of a productive interaction between the TSL-region and its binding site (TBS) in the specificity domain using tRNA precursors and various hairpin-loop model substrates. The different substrates were analyzed with respect to cleavage site recognition, ground-state binding, cleavage as a function of the concentration of Mg(2+) and the rate of cleavage under conditions where chemistry is suggested to be rate limiting using wild-type Escherichia coli RNase P RNA, M1 RNA, and M1 RNA variants with structural changes in the TBS-region. On the basis of our data, we conclude that a productive TSL/TBS interaction results in a conformational change in the M1 RNA substrate complex that has an effect on catalysis. Moreover, it is likely that this conformational change comprises positioning of chemical groups (and Mg(2+)) at and in the vicinity of the cleavage site. Hence, our findings are consistent with an induced-fit mechanism in RNase P RNA-mediated cleavage." @default.
- W1985875854 created "2016-06-24" @default.
- W1985875854 creator A5006359874 @default.
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- W1985875854 date "2007-10-01" @default.
- W1985875854 modified "2023-09-30" @default.
- W1985875854 title "Evidence for Induced Fit in Bacterial RNase P RNA-mediated Cleavage" @default.
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- W1985875854 doi "https://doi.org/10.1016/j.jmb.2007.07.030" @default.
- W1985875854 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17719605" @default.
- W1985875854 hasPublicationYear "2007" @default.
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