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

Satoshi Kimura (), Veerasak Srisuknimit, Kacie L. McCarty, Peter C. Dedon, Philip J. Kranzusch and Matthew K. Waldor ()
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Satoshi Kimura: Brigham and Women’s Hospital
Veerasak Srisuknimit: Brigham and Women’s Hospital
Kacie L. McCarty: Harvard Medical School
Peter C. Dedon: Massachusetts Institution of Technology
Philip J. Kranzusch: Harvard Medical School
Matthew K. Waldor: Brigham and Women’s Hospital

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract 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 (cytidine deaminase and pseudouridylase) and 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.

Date: 2022
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DOI: 10.1038/s41467-022-33714-x

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