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. Author manuscript; available in PMC: 2020 Jul 25.
Published in final edited form as: Cell. 2019 Jul 25;178(3):612–623.e12. doi: 10.1016/j.cell.2019.06.035

Figure 7.

Figure 7.

Group II intron and the spliceosome share mechanistic dynamics. (A) In group II introns the thumb/x domain of the maturase protein promotes splicing by binding to DVI of the RNA and stabilizing the bulged adenosine in the active site to facilitate lariat formation. In the spliceosomal C complex (PDB Accession Code 5LJ5), the RNaseH-like domain of prp8 plays a similar role in binding and transitioning the homologous branch helix through the different stages of splicing (Galej et al., 2016). (B) The DVI helix of the group II intron undergoes a 90° swinging motion between the pre-1r and pre-2r stages of DNA integration. Identical dynamics are observed in the spliceosome in the transition between the C complex (PDB Accession Code 5LJ5) (Galej et al., 2016) and the post-catalytic P (post-P) complex (PDB Accession Code 6QDV) (Fica et al., 2019). The post-P complex and the C complex are structurally homologous to the pre-1r and pre-2r states, respectively. This conserved dynamic motion supports the hypothesis that the spliceosome has evolutionary origins as a group II intron-like retroelement.