A viral ADP-ribosyltransferase attaches RNA chains to host proteins

Maik Wolfram-Schauerte, Nadiia Pozhydaieva, Julia Grawenhoff, Luisa M. Welp, Ivan Silbern, Alexander Wulf, Franziska A. Billau, Timo Glatter, Henning Urlaub, Andres Jäschke () and Katharina Höfer ()
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Maik Wolfram-Schauerte: Max Planck Institute for Terrestrial Microbiology
Nadiia Pozhydaieva: Max Planck Institute for Terrestrial Microbiology
Julia Grawenhoff: Heidelberg University
Luisa M. Welp: Max Planck Institute for Multidisciplinary Sciences
Ivan Silbern: Max Planck Institute for Multidisciplinary Sciences
Alexander Wulf: Max Planck Institute for Multidisciplinary Sciences
Franziska A. Billau: Heidelberg University
Timo Glatter: Max Planck Institute for Terrestrial Microbiology
Henning Urlaub: Max Planck Institute for Multidisciplinary Sciences
Andres Jäschke: Heidelberg University
Katharina Höfer: Max Planck Institute for Terrestrial Microbiology

Nature, 2023, vol. 620, issue 7976, 1054-1062

Abstract: 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 substrate1,2. NAD has previously been identified as a 5′ modification of cellular RNAs3–5. 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 phage RNAs are linked to rS1 in vivo. T4 phages that express an inactive mutant of ModB have a decreased burst size and slowed lysis of E. coli. Our findings reveal a distinct biological role for NAD–RNA, namely the activation of the RNA for enzymatic transfer to proteins. The attachment of specific RNAs to ribosomal proteins might provide a strategy for the phage to modulate the host’s translation machinery. This work reveals a direct connection between RNA modification and post-translational protein modification. ARTs have important roles far beyond viral infections6, so RNAylation may have far-reaching implications.

Date: 2023
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DOI: 10.1038/s41586-023-06429-2

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