About: The RNA polymerase activity of SARS-coronavirus nsp12 is primer dependent

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: The RNA polymerase activity of SARS-coronavirus nsp12 is primer dependent 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	The RNA polymerase activity of SARS-coronavirus nsp12 is primer dependent
Creator	Snijder, Eric Arnold, Jamie Cameron, Craig Te Velthuis, Aartjan Van Den Worm, Sjoerd
Source	Medline; PMC
abstract	An RNA-dependent RNA polymerase (RdRp) is the central catalytic subunit of the RNA-synthesizing machinery of all positive-strand RNA viruses. Usually, RdRp domains are readily identifiable by comparative sequence analysis, but biochemical confirmation and characterization can be hampered by intrinsic protein properties and technical complications. It is presumed that replication and transcription of the ∼30-kb severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) RNA genome are catalyzed by an RdRp domain in the C-terminal part of nonstructural protein 12 (nsp12), one of 16 replicase subunits. However, thus far full-length nsp12 has proven refractory to expression in bacterial systems, which has hindered both the biochemical characterization of coronavirus RNA synthesis and RdRp-targeted antiviral drug design. Here, we describe a combined strategy involving bacterial expression of an nsp12 fusion protein and its in vivo cleavage to generate and purify stable SARS-CoV nsp12 (106 kDa) with a natural N-terminus and C-terminal hexahistidine tag. This recombinant protein possesses robust in vitro RdRp activity, as well as a significant DNA-dependent activity that may facilitate future inhibitor studies. The SARS-CoV nsp12 is primer dependent on both homo- and heteropolymeric templates, supporting the likeliness of a close enzymatic collaboration with the intriguing RNA primase activity that was recently proposed for coronavirus nsp8.
has issue date	2009-10-29(xsd:dateTime)
bibo:doi	10.1093/nar/gkp904
bibo:pmid	19875418
has license	cc-by-nc
sha1sum (hex)	f901f9949a8c6e53727335e92a39707e89965422
schema:url	https://doi.org/10.1093/nar/gkp904
resource representing a document's title	The RNA polymerase activity of SARS-coronavirus nsp12 is primer dependent
has PubMed Central identifier	PMC2800238
has PubMed identifier	19875418
schema:publication	Nucleic Acids Res
resource representing a document's body	covid:f901f9949a8c6e53727335e92a39707e89965422#body_text
is schema:about of	named entity 'IDENTIFIABLE' named entity 'SIGNIFICANT' named entity 'BIOCHEMICAL' named entity 'INTRINSIC' named entity 'ACTIVITY' named entity 'STABLE' named entity 'REPLICATION' named entity 'BUT' named entity 'RDRP' named entity 'REFRACTORY' named entity 'HOMO' named entity 'COMPLICATIONS' named entity 'TEMPLATES' named entity 'PURIFY' named entity 'IN VITRO' named entity 'BIOCHEMICAL CHARACTERIZATION' named entity 'PROTEIN PROPERTIES' named entity 'COLLABORATION' named entity 'FAR' named entity 'HEXAHISTIDINE' named entity 'ITS' named entity 'LENGTH' named entity 'TARGETED' named entity 'INHIBITOR' named entity 'SUBUNIT' named entity 'POSITIVE' named entity 'FUTURE' named entity 'BACTERIAL EXPRESSION' named entity 'RNA VIRUSES' named entity 'BACTERIAL' named entity 'CORONAVIRUS' named entity 'expression' named entity 'cleavage' named entity 'sequence analysis' named entity 'genome' named entity 'coronavirus' named entity 'viruses' named entity 'replication' named entity 'primer' named entity 'RNA POLYMERASE ACTIVITY' named entity 'STRATEGY' named entity 'PRESUMED' named entity 'RNA-DEPENDENT RNA POLYMERASE' named entity 'PRIMASE' named entity 'CATALYTIC' named entity 'PRIMER' named entity 'ENZYMATIC' named entity 'CENTRAL' named entity 'DEPENDENT' named entity 'STRAND' named entity 'COMBINED' named entity 'CLEAVAGE' named entity 'SARS-COV' named entity 'TECHNICAL' named entity 'SARS' named entity 'DEPENDENT' named entity 'PROPOSED' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'DOMAIN' named entity 'PART OF' named entity 'ANTIVIRAL DRUG' named entity 'DESCRIBE' named entity '2430' named entity 'HERE' named entity 'REPLICASE' named entity 'GENERATE' named entity 'PROVEN' named entity 'CLOSE' named entity 'RNA SYNTHESIS' named entity 'SYSTEMS' named entity 'KDA' named entity 'PROTEIN ' named entity 'ONE OF' named entity 'ROBUST' named entity 'NATURAL' named entity 'RECOMBINANT PROTEIN' named entity 'STUDIES'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software