Population
Group II introns (self-splicing ribozymes and retrotransposable elements)
Design
Preclinical
Key result
Protonation of the first residue of the highly-conserved catalytic triad (C358) upon 5'-splice-site scission promotes a reversible structural rearrangement of the active site, facilitating progression to the second step of splicing.
Authors
Loading...
Advances spliceosome mechanism models; extends structural data but leaves open human disease relevance.
Protonation and active site dynamics induced by the first step of splicing facilitate the progression to the second step, paralleling functional data on the spliceosome.
Manigrasso et al. (2020) studied Group II intron splicing. Active site mutations (C358A, C358G, C358U) vs. Wild-type O. iheyensis group II intron was evaluated on Splicing kinetics and structural conformation (toggling). Protonation of the first residue of the highly-conserved catalytic triad (C358) upon 5'-splice-site scission promotes a reversible structural rearrangement of the active site, facilitating progression to the second step of splicing.