A viral ADP-ribosyltransferase attaches RNA chains to host proteins.

ABSTRACT: The mechanisms by which viruses hijack the genetic machinery of the cells they infect are of current interest. When bacteriophage T4 infects Escherichia coli, it uses three different adenosine diphosphate (ADP)-ribosyltransferases (ARTs) to reprogram the transcriptional and translational apparatus of the host by ADP-ribosylation using nicotinamide adenine dinucleotide (NAD) as a substrate^1,2. NAD has previously been identified as a 5' modification of cellular RNAs^3-5. Here we report that the T4 ART ModB accepts not only NAD but also NAD-capped RNA (NAD-RNA) as a substrate and attaches entire RNA chains to acceptor proteins in an 'RNAylation' reaction. ModB specifically RNAylates the ribosomal proteins rS1 and rL2 at defined Arg residues, and selected E. coli and T4 ph

SUBMITTER: Wolfram-Schauerte M 

PROVIDER: S-EPMC10468400 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature