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  A viral ADP-ribosyltransferase attaches RNA chains to host proteins

Wolfram-Schauerte, M., Pozhydaieva, N., Grawenhoff, J., Welp, L. M., Silbern, I., Wulf, A., et al. (2023). A viral ADP-ribosyltransferase attaches RNA chains to host proteins. Nature, 620, 1054-1062. doi:10.1038/s41586-023-06429-2.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000D-BFC0-3 Version Permalink: https://hdl.handle.net/21.11116/0000-000D-BFC1-2
Genre: Journal Article

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s41586-023-06429-2.pdf (Publisher version), 22MB
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 Creators:
Wolfram-Schauerte, Maik, Author
Pozhydaieva, Nadiia, Author
Grawenhoff, Julia, Author
Welp, Luisa M.1, Author           
Silbern, Ivan1, Author           
Wulf, Alexander1, Author           
Billau, Franziska A., Author
Glatter, Timo, Author
Urlaub, Henning1, Author           
Jäschke, Andres, Author
Höfer, Katharina, Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350290              

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 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. NAD has previously been identified as a 5′ modification of cellular RNAs. 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 infections, so RNAylation may have far-reaching implications.

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Language(s): eng - English
 Dates: 2023-08-162023-08-31
 Publication Status: Issued
 Pages: -
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41586-023-06429-2
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Project name : This project has received funding from the European Research Council under the European Union’s Horizon 2020 research and innovation programme (grant 882789 RNACoenzyme, to A.J.) and from the German Research Council (DFG; project 439669440, TRR319, project A02, to A.J.). M.W.-S. is supported by the Studienstiftung des Deutschen Volkes and the Joachim Herz Stiftung. K.H. is supported by the Max Planck Society, Baden-Württemberg Stiftung, Carl-Zeiss-Stiftung and the German Research Council (grant DFG-SPP2330). H.U. is supported by the Max Planck Institute for Multidisciplinary Sciences and by the German Research Council (grants DFG-SPP1935, DFG-SFB1286 and DFG-SFB1565 (project number 469281184)).
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Project name : RNACoenzyme
Grant ID : 882789
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)

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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 620 Sequence Number: - Start / End Page: 1054 - 1062 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238