About: Discovery of an essential nucleotidylating activity associated with a newly delineated conserved domain in the RNA polymerase-containing protein of all nidoviruses

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About: Discovery of an essential nucleotidylating activity associated with a newly delineated conserved domain in the RNA polymerase-containing protein of all nidoviruses Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Discovery of an essential nucleotidylating activity associated with a newly delineated conserved domain in the RNA polymerase-containing protein of all nidoviruses
Creator	Gulyaeva, Anastasia Samborskiy, Dmitry Sidorov, Igor Zevenhoven-Dobbe, Jessika Gorbalenya, Alexander Snijder, Eric Kravchenko, Alexander Lehmann, Kathleen Leontovich, Andrey Posthuma, Clara Overkleeft, Hermen Ruben, Mark Janssen, George Van Veelen, Peter
topic	covid:8adc81255b4ba0eb48cbd7ddfe86f13959f39c7d#this
Source	Medline; PMC
abstract	RNA viruses encode an RNA-dependent RNA polymerase (RdRp) that catalyzes the synthesis of their RNA(s). In the case of positive-stranded RNA viruses belonging to the order Nidovirales, the RdRp resides in a replicase subunit that is unusually large. Bioinformatics analysis of this non-structural protein has now revealed a nidoviral signature domain (genetic marker) that is N-terminally adjacent to the RdRp and has no apparent homologs elsewhere. Based on its conservation profile, this domain is proposed to have nucleotidylation activity. We used recombinant non-structural protein 9 of the arterivirus equine arteritis virus (EAV) and different biochemical assays, including irreversible labeling with a GTP analog followed by a proteomics analysis, to demonstrate the manganese-dependent covalent binding of guanosine and uridine phosphates to a lysine/histidine residue. Most likely this was the invariant lysine of the newly identified domain, named nidovirus RdRp-associated nucleotidyltransferase (NiRAN), whose substitution with alanine severely diminished the described binding. Furthermore, this mutation crippled EAV and prevented the replication of severe acute respiratory syndrome coronavirus (SARS-CoV) in cell culture, indicating that NiRAN is essential for nidoviruses. Potential functions supported by NiRAN may include nucleic acid ligation, mRNA capping and protein-primed RNA synthesis, possibilities that remain to be explored in future studies.
has issue date	2015-09-30(xsd:dateTime)
bibo:doi	10.1093/nar/gkv838
bibo:pmid	26304538
has license	cc-by-nc
sha1sum (hex)	8adc81255b4ba0eb48cbd7ddfe86f13959f39c7d
schema:url	https://doi.org/10.1093/nar/gkv838
resource representing a document's title	Discovery of an essential nucleotidylating activity associated with a newly delineated conserved domain in the RNA polymerase-containing protein of all nidoviruses
has PubMed Central identifier	PMC4787807
has PubMed identifier	26304538
schema:publication	Nucleic Acids Res
resource representing a document's body	covid:8adc81255b4ba0eb48cbd7ddfe86f13959f39c7d#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/8adc81255b4ba0eb48cbd7ddfe86f13959f39c7d
is schema:about of	named entity 'ACTIVITY' named entity 'ASSOCIATED WITH' named entity 'NAMED' named entity 'RNA-DEPENDENT RNA POLYMERASE' named entity 'SUBUNIT' named entity 'LIGATION' named entity 'ALANINE' named entity 'BELONGING' named entity 'NON-' named entity 'POSITIVE' named entity 'FUTURE' named entity 'SEVERELY' named entity 'RNA SYNTHESIS' named entity 'INVARIANT' named entity 'SUBSTITUTION' named entity 'DIFFERENT' named entity 'IDENTIFIED' named entity 'EQUINE ARTERITIS VIRUS' named entity 'SUPPORTED' named entity 'PRIMED' named entity 'DIMINISHED' named entity 'PROTEIN' named entity 'RDRP' named entity 'STRUCTURAL PROTEIN' named entity 'NUCLEIC ACID' named entity 'ITS' named entity 'positive-stranded' named entity 'demonstrate' named entity 'subunit' named entity 'apparent' named entity 'genetic marker' named entity 'binding' named entity 'nonstructural protein' named entity 'belonging' named entity 'DELINEATED' named entity 'NEWLY' named entity 'PROTEIN ' named entity 'CONSERVATION' named entity 'NUCLEOTIDYLATION' named entity 'ANALOG' named entity 'NEWLY' named entity 'INDICATING' named entity 'THEIR' named entity 'ORDER NIDOVIRALES' named entity 'ESSENTIAL' named entity 'ARTERIVIRUS' named entity 'COVALENT BINDING' named entity 'RNA POLYMERASE' named entity 'CONSERVED' named entity 'DISCOVERY' named entity 'PROTEIN ' named entity 'DOMAIN' named entity 'DOMAIN' named entity 'RNA' named entity 'INCLUDE' named entity 'ENCODE' named entity 'IRREVERSIBLE' named entity 'CASE' named entity '28S' named entity 'MANGANESE' named entity 'CRIPPLED' named entity 'LYSINE' named entity 'REPLICASE' named entity 'BIOCHEMICAL' named entity 'GUANOSINE' named entity 'SYNTHESIS'

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