About: Cellular 5′-3′ mRNA Exonuclease Xrn1 Controls Double-stranded RNA Accumulation and Anti-Viral Responses

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About: Cellular 5′-3′ mRNA Exonuclease Xrn1 Controls Double-stranded RNA Accumulation and Anti-Viral Responses Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Cellular 5′-3′ mRNA Exonuclease Xrn1 Controls Double-stranded RNA Accumulation and Anti-Viral Responses
Creator	Burgess, & Mohr,
Source	Elsevier; Medline; PMC
abstract	By accelerating global mRNA decay, many viruses impair host protein synthesis, limiting host defenses and stimulating virus mRNA translation. Vaccinia virus (VacV) encodes two decapping enzymes (D9, D10) that remove protective 5′ caps on mRNAs, presumably generating substrates for degradation by the host exonuclease Xrn1. Surprisingly, we find VacV infection of Xrn1-depleted cells inhibits protein synthesis, compromising virus growth. These effects are aggravated by D9-deficiency and dependent upon a virus transcription factor required for intermediate and late mRNA biogenesis. Considerable double-stranded RNA (dsRNA) accumulation in Xrn1-depleted cells is accompanied by activation of host dsRNA-responsive defenses controlled by PKR and 2′-5′-oligoadenylate synthetase (OAS), which respectively inactivate the translation initiation factor eIF2 and stimulate RNA cleavage by RNase L. This proceeds despite VacV-encoded PKR and RNase L antagonists being present. Moreover, Xrn1-depletion sensitizes uninfected cells to dsRNA treatment. Thus, Xrn1 is a cellular factor regulating dsRNA accumulation and dsRNA-responsive innate immune effectors.
has issue date	2015-03-01(xsd:dateTime)
bibo:doi	10.1016/j.chom.2015.02.003
bibo:pmid	25766294
has license	hybrid-oa
sha1sum (hex)	473fbfa4949e8349434157a9f65687087176e605
schema:url	https://doi.org/10.1016/j.chom.2015.02.003
resource representing a document's title	Cellular 5′-3′ mRNA Exonuclease Xrn1 Controls Double-stranded RNA Accumulation and Anti-Viral Responses
has PubMed Central identifier	PMC4826345
has PubMed identifier	25766294
schema:publication	Cell Host & Microbe
resource representing a document's body	covid:473fbfa4949e8349434157a9f65687087176e605#body_text
is schema:about of	named entity 'permissions' named entity 'Elsevier' named entity 'database' named entity 'original source' named entity 'Double-Stranded' named entity 'RNA' named entity 'eIF2a' named entity 'Xrn1' named entity 'viral DNA' named entity 'dsRNA' named entity 'dsRNA' named entity 'DNA viruses' named entity 'K3L' named entity 'post-transcriptionally' named entity 'Xrn1' named entity 'genome-wide' named entity 'Triton X-100' named entity 'gene expression profile' named entity 'radiolabeled' named entity 'protein synthesis' named entity 'Xrn1' named entity 'secondary antibody' named entity 'mRNAs' named entity 'binding protein' named entity 'siRNA' named entity 'RNase' named entity 'pH 8' named entity '12,000' named entity 'arms race' named entity 'protein synthesis' named entity 'exonuclease' named entity 'exonuclease' named entity 'siRNA' named entity 'Xrn1' named entity 'GCN2' named entity 'Molecular mass' named entity 'Xrn1' named entity 'Cell Signaling Technology' named entity 'coronaviruses' named entity 'infection control' named entity 'mRNA' named entity 'RNase' named entity 'viral DNA' named entity 'siRNAs' named entity 'binding protein' named entity 'phospho' named entity 'protein synthesis' named entity 'protein synthesis' named entity 'Xrn1' named entity 'pseudosubstrate' named entity 'rRNA' named entity 'siRNA' named entity 'infection' named entity 'mRNAs' named entity 'infection' named entity 'inhibition of protein synthesis' named entity 'DNA virus' named entity 'cross-linked' named entity 'open reading frames' named entity 'DMEM' named entity 'RNase L' named entity '2006, 2007' named entity 'binding protein' named entity 'actin' named entity 'homeostasis' named entity 'phosphorylated' named entity 'eIF2a' named entity 'antibody' named entity 'virus' named entity 'decapping' named entity 'dsRNA' named entity 'Xrn1' named entity 'host defenses' named entity 'dsRNA' named entity 'metabolically' named entity 'Xrn1' named entity 'protein synthesis' named entity 'interferon' named entity 'agarose beads' named entity 'protein synthesis'

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