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• W2007788169 abstract "Abstract We analyzed processing of precursor tRNAs carrying a single 2′-deoxy, 2′-OCH 3 , or locked nucleic acid (LNA) modification at G+1 by Escherichia coli RNase P RNA in the absence and presence of its protein cofactor. The extra methyl or methylene group caused a substrate binding defect, which was rescued at higher divalent metal ion (M 2+ ) concentrations (more efficiently with Mn 2+ than Mg 2+ ), and had a minor effect on cleavage chemistry at saturating M 2+ concentrations. The 2′-OCH 3 and LNA modification at G+1 resulted in higher metal ion cooperativity for substrate binding to RNase P RNA without affecting cleavage site selection. This indicates disruption of an M 2+ binding site in enzyme-substrate complexes, which is compensated for by occupation of alternative M 2+ binding sites of lower affinity. The 2′-deoxy modification at G+1 caused at most a two-fold decrease in the cleavage rate; this mild defect relative to 2′-OCH 3 and LNA at G+1 indicates that the defect caused by the latter two is steric in nature. We propose that the 2′-hydroxyl at G+1 in the substrate is in the immediate vicinity of the M 2+ cluster at the phosphates of A67 to U69 in helix P4 of E. coli RNase P RNA." @default.
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• W2007788169 date "2007-07-01" @default.
• W2007788169 modified "2023-09-25" @default.
• W2007788169 title "A 2′-methyl or 2′-methylene group at G+1 in precursor tRNA interferes with Mg²⁺ binding at the enzyme-substrate interface in E-S complexes of <i>E. coli</i> RNase P" @default.
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• W2007788169 doi "https://doi.org/10.1515/bc.2007.095" @default.
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