Chemoproteomic discovery of a human RNA ligase

Yizhi Yuan, Florian M. Stumpf, Lisa A. Schlor, Olivia P. Schmidt, Philip Saumer, Luisa B. Huber, Matthias Frese, Eva Höllmüller, Martin Scheffner, Florian Stengel, Kay Diederichs and Andreas Marx ()
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Yizhi Yuan: University of Konstanz
Florian M. Stumpf: University of Konstanz
Lisa A. Schlor: University of Konstanz
Olivia P. Schmidt: University of Konstanz
Philip Saumer: University of Konstanz
Luisa B. Huber: University of Konstanz
Matthias Frese: University of Konstanz
Eva Höllmüller: University of Konstanz
Martin Scheffner: University of Konstanz
Florian Stengel: University of Konstanz
Kay Diederichs: University of Konstanz
Andreas Marx: University of Konstanz

Nature Communications, 2023, vol. 14, issue 1, 1-12

Abstract: Abstract RNA ligases are present across all forms of life. While enzymatic RNA ligation between 5′-PO4 and 3′-OH termini is prevalent in viruses, fungi, and plants, such RNA ligases are yet to be identified in vertebrates. Here, using a nucleotide-based chemical probe targeting human AMPylated proteome, we have enriched and identified the hitherto uncharacterised human protein chromosome 12 open reading frame 29 (C12orf29) as a human enzyme promoting RNA ligation between 5′-PO4 and 3′-OH termini. C12orf29 catalyses ATP-dependent RNA ligation via a three-step mechanism, involving tandem auto- and RNA AMPylation. Knock-out of C12ORF29 gene impedes the cellular resilience to oxidative stress featuring concurrent RNA degradation, which suggests a role of C12orf29 in maintaining RNA integrity. These data provide the groundwork for establishing a human RNA repair pathway.

Date: 2023
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DOI: 10.1038/s41467-023-36451-x

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