Reactivity-dependent profiling of RNA 5-methylcytidine dioxygenases

A. Emilia Arguello; Ang Li; Xuemeng Sun; Tanner W. Eggert; Elisabeth Mairhofer; Ralph E. Kleiner

doi:10.1038/s41467-022-31876-2

Nature Communications (Jul 2022)

Reactivity-dependent profiling of RNA 5-methylcytidine dioxygenases

A. Emilia Arguello,
Ang Li,
Xuemeng Sun,
Tanner W. Eggert,
Elisabeth Mairhofer,
Ralph E. Kleiner

Affiliations

A. Emilia Arguello: Department of Chemistry, Princeton University
Ang Li: Department of Chemistry, Princeton University
Xuemeng Sun: Department of Chemistry, Princeton University
Tanner W. Eggert: Department of Chemistry, Princeton University
Elisabeth Mairhofer: Department of Chemistry, Princeton University
Ralph E. Kleiner: Department of Chemistry, Princeton University

DOI: https://doi.org/10.1038/s41467-022-31876-2
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 17

Abstract

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Kleiner and co-workers profile RNA 5-methylcytidine (m5C) dioxygenase enzymes using an activity-based metabolic probing strategy. They reveal ALKBH1 as the major 5-formylcytidine (f5C) writer and characterize modification sites across mRNA and tRNA.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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