Sequential action of a tRNA base editor in conversion of cytidine to pseudouridine

By S. Kimura, Veerasak Srisuknimit, K. McCarty, P. Dedon, P. Kranzusch, M. Waldor. 2022

13 citations recorded by the source corpus.

Post-transcriptional RNA editing modulates gene expression in a condition-dependent fashion. We recently discovered C-to-Ψ editing in Vibrio cholerae tRNA. Here, we characterize the biogenesis, regulation, and functions of this previously undescribed RNA editing process. We show that an enzyme, TrcP, mediates the editing of C-to-U followed by the conversion of U to Ψ, consecutively. AlphaFold-2 predicts that TrcP consists of two globular domains, including a novel cytidine deaminase and a pseudouridylase, along with a long helical domain. The latter domain tethers tRNA substrates during both the C-to-U editing and pseudouridylation, likely enabling a substrate channeling mechanism for efficient catalysis all the way to the terminal product. C-to-Ψ editing both requires and suppresses other modifications, creating an interdependent network of modifications in the tRNA anticodon loop that facilitates coupling of tRNA modification states to iron availability. Our findings provide mechanistic insights into an RNA editing process that likely promotes environmental adaptation.

Subfields: Molecular Biology

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In Molecular Biology

1. Yi Zhao
2. Zhenyu Yang
3. Runsheng Chen
4. Xiaoxi Zeng

Citations in the corpus

• AlphaFold2 and its applications in the fields of biology and medicine (2023, background): “In a recent study, Kimura et al. 156 characterized the C-to-Ψ editing mechanisms.”