Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation (RNA-Seq)

ABSTRACT: Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation (RNA-Seq)

PROVIDER: PRJNA1065926 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR27597248_1.fastq.gz	Fastqsanger.gz
	SRR27597248_2.fastq.gz	Fastqsanger.gz
	SRR27597249_1.fastq.gz	Fastqsanger.gz
	SRR27597249_2.fastq.gz	Fastqsanger.gz
	SRR27597250_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 16

Similar Datasets

Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation (RNA-Seq)

Project description:Host-pathogen conflicts are crucibles of molecular innovation. Selection for immunity to pathogens has driven the evolution of sophisticated immunity mechanisms throughout biology, including in bacteria that must evade their viral predators known as bacteriophages. Here, we characterize a toxin-antitoxin-chaperone system, CmdTAC, in Escherichia coli that provides robust defense against infection by T4 phage. During infection, newly synthesized capsid protein triggers dissociation of the chaperone CmdC from the CmdTAC complex, leading to destabilization and degradation of the antitoxin CmdA, with consequent liberation of the toxin CmdT, an ADP-ribosyltransferase. Strikingly, CmdT does not target a protein, DNA, or structured RNA, the known targets of other ADP-ribosyltransferases. Instead, CmdT modifies the N6 position of adenine in GA dinucleotides within single-stranded RNAs to robustly block mRNA translation and viral replication. Our work reveals both a new mechanism of anti-phage defense and a new class of ADP-ribosyltransferases that targets mRNA.

2024-03-09 | GSE253513 | GEO

Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation

Project description:Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation

| PRJNA1065921 | ENA

Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation (RIP-Seq in vivo)

2024-03-09 | GSE253512 | GEO

Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation (RIP-Seq in vitro)

2024-03-09 | GSE253511 | GEO

Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation (RIP-Seq in vivo)

Project description:Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation (RIP-Seq in vivo)

| PRJNA1065924 | ENA

Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation (RIP-Seq in vitro)

Project description:Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation (RIP-Seq in vitro)

| PRJNA1065925 | ENA

Anti-viral defense by an ADP-ribosyltransferase that targets mRNA to block translation

Project description:This SuperSeries is composed of the SubSeries listed below.

2024-03-09 | GSE253514 | GEO

A viral ADP-ribosyltransferase attaches RNA chains to host proteins

Project description:A viral ADP-ribosyltransferase attaches RNA chains to host proteins

| PRJNA885396 | ENA

A viral ADP-ribosyltransferase attaches RNA chains to host proteins

Project 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 through ADP-ribosylation using nicotinamide adenine dinucleotide (NAD) as substrate. Recently, NAD was identified as a 5’-modification of cellular RNAs. Here, we report that T4 ART ModB accepts not only NAD but also NAD-capped RNA (NAD-RNA) as substrate and attaches entire RNA chains to acceptor proteins in an “RNAylation” reaction. ModB specifically RNAylates ribosomal proteins rS1 and rL2 at defined arginine residues, and selected E. coli and T4 phage RNAs are linked to rS1 in vivo. T4 phages that express an inactive mutant of ModB show a decreased burst size and slowed lysis of E. coli. Our findings reveal a distinct biological role of NAD-RNA, namely 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 exemplifies the first direct connection between RNA modification and post-translational protein modification. As ARTs play important roles far beyond viral infections, RNAylation may have far-reaching implications.

2023-05-25 | GSE214431 | GEO

ADP

Project description:ADP array data, comprised of 2217 samples of Asian ancestry (excluding the Japanese population from ADP). Samples were genotyped on different Illumina or Affy platform.

| EGAD00010001491 | EGA

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data