PXD038910

PXD038910 is an original dataset announced via ProteomeXchange.

Title	A viral ADP-ribosyltransferase attaches RNA chains to host proteins
Description	The mechanisms by which viruses hijack their host’s genetic machinery are of current interest. When bacteriophage T4 infects Escherichia coli, three different ARTs (ADP-ribosyltransferases) reprogram the host’s transcriptional and translational apparatus 1,2 through ADP-ribosylation using nicotinamide adenine dinucleotide (NAD) as substrate. Recently, NAD was identified as a 5’-modification of cellular RNAs 3-5. Here, we report that the bacteriophage T4 ART ModB accepts not only NAD but also NAD-capped RNA (NAD-RNA) as substrate, linking entire RNA chains to acceptor proteins in an “RNAylation” reaction. We discovered that ModB specifically RNAylates ribosomal proteins rS1 and rL2. By mass spectrometric (MS) analysis we identified arginine residues of rS1 and rL2 as RNAylation sites. Furthermore, we identified specific E. coli and T4 phage RNAs, which are covalently linked to rS1 in vivo. T4 phages expressing an inactive mutant of ModB show a decreased burst size and a decelerated lysis of E. coli during T4 infection. The attachment of specific RNAs to ribosomal proteins might provide a strategy for the phage to modulate the host’s translation machinery. Our findings reveal a distinct biological role of NAD-RNA, namely activation of the RNA for enzymatic transfer. This work exemplifies the first direct connection between RNA modification and post-translational protein modification. As ARTs play important roles far beyond viral infections 6, RNAylation may have far-reaching implications.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_09:05:04.374.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Luisa Welp
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2022-12-19 03:12:28	ID requested
1	2023-06-01 01:30:26	announced
2	2023-09-06 00:35:59	announced	2023-09-06: Updated project metadata.
⏵ 3	2023-11-14 09:05:05	announced	2023-11-14: Updated project metadata.

Wolfram-Schauerte M, Pozhydaieva N, Grawenhoff J, Welp LM, Silbern I, Wulf A, Billau FA, Glatter T, Urlaub H, J, ä, schke A, H, ö, fer K, A viral ADP-ribosyltransferase attaches RNA chains to host proteins. Nature, 620(7976):1054-1062(2023) [pubmed]

submitter keyword: Escherichia coli,RNAylation, T4 phage, LC-MS/MS

Dr. Katharina Höfer
contact affiliation	SYNMIKRO, Zentrum für Synthetische Mikrobiologie, Philipps Universität Marburg, Karl-von-Frisch-Str. 14, 35043 Marburg, Germany Max-Planck-Institut für Terrestrische Mikrobiologie, Karl-von-Frisch Straße 16, 35043 Marburg, Germany
contact email	Katharina.Hoefer@synmikro.mpi-marburg.mpg.de
lab head
Luisa Welp
contact affiliation	Max-Planck-Institute for Biophysical Chemistry
contact email	lwelp@gwdg.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/06/PXD038910

PRIDE project URI

• PRIDE
  1. PXD038910
     1. Label: PRIDE project
     2. Name: A viral ADP-ribosyltransferase attaches RNA chains to host proteins