Structure-based insights into self-cleavage by a four-way junctional twister-sister ribozyme Journal Article
| Authors: | Zheng, L.; Mairhofer, E.; Teplova, M.; Zhang, Y.; Ma, J.; Patel, D. J.; Micura, R.; Ren, A. |
| Article Title: | Structure-based insights into self-cleavage by a four-way junctional twister-sister ribozyme |
| Abstract: | Here we report on the crystal structure and cleavage assays of a four-way junctional twister-sister self-cleaving ribozyme. Notably, 11 conserved spatially separated loop nucleotides are brought into close proximity at the ribozyme core through long-range interactions mediated by hydrated Mg2+ cations. The C62-A63 step at the cleavage site adopts a splayed-apart orientation, with flexible C62 directed outwards, whereas A63 is directed inwards and anchored by stacking and hydrogen-bonding interactions. Structure-guided studies of key base, sugar, and phosphate mutations in the twister-sister ribozyme, suggest contributions to the cleavage chemistry from interactions between a guanine at the active site and the non-bridging oxygen of the scissile phosphate, a feature found previously also for the related twister ribozyme. Our four-way junctional pre-catalytic structure differs significantly in the alignment at the cleavage step (splayed-apart vs. base-stacked) and surrounding residues and hydrated Mg2+ ions relative to a reported three-way junctional pre-catalytic structure of the twister-sister ribozyme. © 2017 The Author(s). |
| Journal Title: | Nature Communications |
| Volume: | 8 |
| ISSN: | 2041-1723 |
| Publisher: | Nature Publishing Group |
| Date Published: | 2017-10-30 |
| Start Page: | 1180 |
| Language: | English |
| DOI: | 10.1038/s41467-017-01276-y |
| PROVIDER: | scopus |
| PMCID: | PMC5660989 |
| PUBMED: | 29081514 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 4 December 2017 -- Source: Scopus |
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