Cryo-EM structures of full-length Tetrahymena ribozyme at 3.1 Å resolution

Zhaoming Su (), Kaiming Zhang, Kalli Kappel, Shanshan Li, Michael Z. Palo, Grigore D. Pintilie, Ramya Rangan, Bingnan Luo, Yuquan Wei, Rhiju Das () and Wah Chiu ()
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Zhaoming Su: Sichuan University
Kaiming Zhang: Stanford University
Kalli Kappel: Stanford University
Shanshan Li: Stanford University
Michael Z. Palo: Stanford University
Grigore D. Pintilie: Stanford University
Ramya Rangan: Stanford University
Bingnan Luo: Sichuan University
Yuquan Wei: Sichuan University
Rhiju Das: Stanford University
Wah Chiu: Stanford University

Nature, 2021, vol. 596, issue 7873, 603-607

Abstract: Abstract Single-particle cryogenic electron microscopy (cryo-EM) has become a standard technique for determining protein structures at atomic resolution1–3. However, cryo-EM studies of protein-free RNA are in their early days. The Tetrahymena thermophila group I self-splicing intron was the first ribozyme to be discovered and has been a prominent model system for the study of RNA catalysis and structure–function relationships4, but its full structure remains unknown. Here we report cryo-EM structures of the full-length Tetrahymena ribozyme in substrate-free and bound states at a resolution of 3.1 Å. Newly resolved peripheral regions form two coaxially stacked helices; these are interconnected by two kissing loop pseudoknots that wrap around the catalytic core and include two previously unforeseen (to our knowledge) tertiary interactions. The global architecture is nearly identical in both states; only the internal guide sequence and guanosine binding site undergo a large conformational change and a localized shift, respectively, upon binding of RNA substrates. These results provide a long-sought structural view of a paradigmatic RNA enzyme and signal a new era for the cryo-EM-based study of structure–function relationships in ribozymes.

Date: 2021
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DOI: 10.1038/s41586-021-03803-w

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