Bridging the gap: RNAylation conjugates RNAs to proteins.

In nature, the majority of known RNA-protein interactions are transient. Our recent study has depicted a novel mechanism known as RNAylation, which covalently links proteins and RNAs. This novel modification bridges the realms of RNA and protein modifications. This review specifically explores RNAylation catalyzed by bacteriophage T4 ADP-ribosyltransferase ModB, with a focus on its protein targets and RNA substrates in the context of Escherichia coli -bacteriophage T4 interaction. Additionally, we discuss the biological significance of RNAylation and present perspectives on RNAylation as a versatile bioconjugation strategy for RNAs and proteins. [Display omitted] • RNAs and proteins are covalently linked in vivo by an RNAylation reaction. • RNAylation is catalyzed by the bacteriophage T4 ADP-ribosyltransferase ModB. • NAD-capped RNAs are the substrates of ModB for RNAylation. • Ribosomal proteins are specifically RNAylated in vivo. • RNAylation may be used as a bioconjugation strategy to engineer RNA-protein conjugates. [ABSTRACT FROM AUTHOR]