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• W2152051520 endingPage "51" @default.
• W2152051520 startingPage "38" @default.
• W2152051520 abstract "Metal ions interact with RNA to enhance folding, stabilize structure, and, in some cases, facilitate catalysis. Assigning functional roles to specifically bound metal ions presents a major challenge in analyzing the catalytic mechanisms of ribozymes. Bacillus subtilis ribonuclease P (RNase P), composed of a catalytically active RNA subunit (PRNA) and a small protein subunit (P protein), catalyzes the 5'-end maturation of precursor tRNAs (pre-tRNAs). Inner-sphere coordination of divalent metal ions to PRNA is essential for catalytic activity but not for the formation of the RNase P x pre-tRNA (enzyme-substrate, ES) complex. Previous studies have demonstrated that this ES complex undergoes an essential conformational change (to the ES* conformer) before the cleavage step. Here, we show that the ES* conformer is stabilized by a high-affinity divalent cation capable of inner-sphere coordination, such as Ca(II) or Mg(II). Additionally, a second, lower-affinity Mg(II) activates cleavage catalyzed by RNase P. Structural changes that occur upon binding Ca(II) to the ES complex were determined by time-resolved Förster resonance energy transfer measurements of the distances between donor-acceptor fluorophores introduced at specific locations on the P protein and pre-tRNA 5' leader. These data demonstrate that the 5' leader of pre-tRNA moves 4 to 6 A closer to the PRNA x P protein interface during the ES-to-ES* transition and suggest that the metal-dependent conformational change reorganizes the bound substrate in the active site to form a catalytically competent ES* complex." @default.
• W2152051520 created "2016-06-24" @default.
• W2152051520 creator A5013264305 @default.
• W2152051520 creator A5016259851 @default.
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• W2152051520 creator A5066163621 @default.
• W2152051520 creator A5077561866 @default.
• W2152051520 creator A5087512728 @default.
• W2152051520 date "2010-07-01" @default.
• W2152051520 modified "2023-10-17" @default.
• W2152051520 title "A Divalent Cation Stabilizes the Active Conformation of the B. subtilis RNase P·Pre-tRNA Complex: A Role for an Inner-Sphere Metal Ion in RNase P" @default.
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• W2152051520 doi "https://doi.org/10.1016/j.jmb.2010.04.050" @default.
• W2152051520 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2939038" @default.
• W2152051520 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20434461" @default.
• W2152051520 hasPublicationYear "2010" @default.
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