About: Human OAS1 activation is highly dependent on both RNA sequence and context of activating RNA motifs

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About: Human OAS1 activation is highly dependent on both RNA sequence and context of activating RNA motifs 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	Human OAS1 activation is highly dependent on both RNA sequence and context of activating RNA motifs
Creator	Lowen, Anice Conn, Graeme Danzy, Shamika Park, Esther Schwartz, Samantha Vachon, Virginia
Source	Medline; PMC
abstract	2′-5′-Oligoadenylate synthetases (OAS) are innate immune sensors of cytosolic double-stranded RNA (dsRNA) and play a critical role in limiting viral infection. dsRNA binding induces allosteric structural changes in OAS1 that reorganize its catalytic center to promote synthesis of 2′-5′-oligoadenylate and thus activation of endoribonuclease L. Specific RNA sequences and structural motifs can also enhance activation of OAS1 through currently undefined mechanisms. To better understand these drivers of OAS activation, we tested the impact of defined sequence changes within a short dsRNA that strongly activates OAS1. Both in vitro and in human A549 cells, appending a 3′-end single-stranded pyrimidine (3′-ssPy) can strongly enhance OAS1 activation or have no effect depending on its location, suggesting that other dsRNA features are necessary for correct presentation of the motif to OAS1. Consistent with this idea, we also find that the dsRNA binding position is dictated by an established consensus sequence (WWN(9)WG). Unexpectedly, however, not all sequences fitting this consensus activate OAS1 equivalently, with strong dependence on the identity of both partially conserved (W) and non-conserved (N(9)) residues. A picture thus emerges in which both specific RNA features and the context in which they are presented dictate the ability of short dsRNAs to activate OAS1.
has issue date	2020-07-27(xsd:dateTime)
bibo:doi	10.1093/nar/gkaa513
bibo:pmid	32678884
has license	cc-by
sha1sum (hex)	06d43134d3069227e19017b6e9e9744e15532d4d
schema:url	https://doi.org/10.1093/nar/gkaa513
resource representing a document's title	Human OAS1 activation is highly dependent on both RNA sequence and context of activating RNA motifs
has PubMed Central identifier	PMC7367156
has PubMed identifier	32678884
schema:publication	Nucleic Acids Res
resource representing a document's body	covid:06d43134d3069227e19017b6e9e9744e15532d4d#body_text
is schema:about of	named entity 'activation' named entity 'enhance' named entity 'presented' named entity 'motif' named entity 'sequences' named entity 'highly' named entity 'PROMOTE' named entity 'DRIVERS' named entity 'SEQUENCES' named entity 'induces' named entity 'viral infection' named entity 'activates' named entity 'cells' named entity 'position' named entity 'sequences' named entity 'dsRNA' named entity 'identity' named entity 'dsRNA' named entity 'enhance' named entity 'fitting' named entity 'specific' named entity 'ability' named entity 'Human' named entity 'dsRNA' named entity 'structural motifs' named entity 'single-stranded' named entity 'endoribonuclease' named entity 'OAS1' named entity 'dsRNA' named entity 'OAS1' named entity 'dsRNA' named entity 'A549' named entity 'dsRNA' named entity 'motif' named entity 'OAS1' named entity 'RNA' named entity 'binding' named entity 'multiple sclerosis' named entity 'OAS1' named entity 'OAS1' named entity 'dsRNA' named entity 'Base Pair' named entity 'dsRNA' named entity 'motif' named entity 'RNAs' named entity 'splicing' named entity 'crosslinked' named entity 'dsRNA' named entity 'cleavage' named entity 'A-form helix' named entity 'A-form helix' named entity 'OAS1' named entity 'guanosine' named entity 'dsRNA' named entity 'Escherichia coli' named entity 'binding affinity' named entity 'dsRNA' named entity 'GE Healthcare' named entity 'GraphPad Prism' named entity 'non-linear regression' named entity 'A549' named entity 'thioU' named entity 'RNA' named entity 'polymerization' named entity 'OAS1' named entity 'OAS1' named entity '1, 2' named entity 'crystal structure' named entity 'isoforms' named entity 'enzyme' named entity 'OAS1' named entity 'OAS1' named entity 'motif' named entity 'A549' named entity 'RNase L' named entity 'base pair'

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