Metals induce transient folding and activation of the twister ribozyme.

ABSTRACT: Twister is a small ribozyme present in almost all kingdoms of life that rapidly self-cleaves in variety of divalent metal ions. We used activity assays, bulk FRET and single-molecule FRET (smFRET) to understand how different metal ions promote folding and self-cleavage of the Oryza sativa twister ribozyme. Although most ribozymes require additional Mg²⁺ for catalysis, twister inverts this expectation, requiring 20-30 times less Mg²⁺ to self-cleave than to fold. Transition metals such as Co²⁺, Ni²⁺ and Zn²⁺ activate twister more efficiently than Mg²⁺ ions. Although twister is fully active in ≤ 0.5 mM MgCl₂, smFRET experiments showed that the ribozyme visits the folded state infrequently under these conditions. Comp

SUBMITTER: Panja S 

PROVIDER: S-EPMC5605428 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature