Structure-based insights into self-cleavage by a four-way junctional twister-sister ribozyme

Luqian Zheng, Elisabeth Mairhofer, Marianna Teplova, Ye Zhang, Jinbiao Ma, Dinshaw J. Patel, Ronald Micura () and Aiming Ren ()
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Luqian Zheng: Zhejiang University
Elisabeth Mairhofer: Leopold Franzens University
Marianna Teplova: Structural Biology Program, Memorial Sloan-Kettering Cancer Center
Ye Zhang: Zhejiang University
Jinbiao Ma: Fudan University
Dinshaw J. Patel: Structural Biology Program, Memorial Sloan-Kettering Cancer Center
Ronald Micura: Leopold Franzens University
Aiming Ren: Zhejiang University

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: 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.

Date: 2017
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DOI: 10.1038/s41467-017-01276-y

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