About: The methyltransferase domain of the Sudan ebolavirus L protein specifically targets internal adenosines of RNA substrates, in addition to the cap structure

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About: The methyltransferase domain of the Sudan ebolavirus L protein specifically targets internal adenosines of RNA substrates, in addition to the cap structure 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 methyltransferase domain of the Sudan ebolavirus L protein specifically targets internal adenosines of RNA substrates, in addition to the cap structure
Creator	Canard, Bruno Decroly, Etienne Coutard, Bruno Vasseur, Jean-Jacques Martin, Baptiste Grimes, Jonathan Paesen, Guido Oise Debart, Franç Guez, Théo
Source	Medline; PMC
abstract	Mononegaviruses, such as Ebola virus, encode an L (large) protein that bears all the catalytic activities for replication/transcription and RNA capping. The C-terminal conserved region VI (CRVI) of L protein contains a K-D-K-E catalytic tetrad typical for 2’O methyltransferases (MTase). In mononegaviruses, cap-MTase activities have been involved in the 2’O methylation and N7 methylation of the RNA cap structure. These activities play a critical role in the viral life cycle as N7 methylation ensures efficient viral mRNA translation and 2’O methylation hampers the detection of viral RNA by the host innate immunity. The functional characterization of the MTase+CTD domain of Sudan ebolavirus (SUDV) revealed cap-independent methyltransferase activities targeting internal adenosine residues. Besides this, the MTase+CTD also methylates, the N7 position of the cap guanosine and the 2’O position of the n1 guanosine provided that the RNA is sufficiently long. Altogether, these results suggest that the filovirus MTases evolved towards a dual activity with distinct substrate specificities. Whereas it has been well established that cap-dependent methylations promote protein translation and help to mimic host RNA, the characterization of an original cap-independent methylation opens new research opportunities to elucidate the role of RNA internal methylations in the viral replication.
has issue date	2018-09-06(xsd:dateTime)
bibo:doi	10.1093/nar/gky637
bibo:pmid	30192980
has license	cc-by-nc
sha1sum (hex)	abb4c06114edb9aa57132be9201478ac965a56ba
schema:url	https://doi.org/10.1093/nar/gky637
resource representing a document's title	The methyltransferase domain of the Sudan ebolavirus L protein specifically targets internal adenosines of RNA substrates, in addition to the cap structure
has PubMed Central identifier	PMC6125687
has PubMed identifier	30192980
schema:publication	Nucleic Acids Res
resource representing a document's body	covid:abb4c06114edb9aa57132be9201478ac965a56ba#body_text
is schema:about of	named entity 'methyltransferase' named entity 'cap' covid:arg/abb4c06114edb9aa57132be9201478ac965a56ba named entity 'opens' named entity 'innate' named entity 'protein translation' named entity 'viral' named entity 'targeting' named entity 'mimic' named entity 'substrate specificities' named entity 'methylation' named entity 'methylation' named entity 'methyltransferase' named entity 'critical role' named entity 'mononegaviruses' named entity 'protein' named entity 'RNA' named entity 'methyltransferase' named entity 'Perkin Elmer' named entity 'substrates' named entity 'epigenetic' named entity 'RNA' named entity 'viral RNA replication' named entity 'Perkin Elmer' named entity 'glycerol' named entity 'ethanol' named entity '30 mM' named entity 'RNA' named entity 'RNA' named entity 'RNA' named entity 'covalently bound' named entity 'dengue virus' named entity 'methylation' named entity 'substrates' named entity 'IEX' named entity 'RNA' named entity 'RNAs' named entity 'RNA-dependent RNA polymerase' named entity 'intracellular' named entity 'adenosines' named entity 'Bundibugyo' named entity 'NaCl' named entity 'methylation' named entity 'nucleotides' named entity 'Tai Forest ebolavirus' named entity 'RNAs' named entity 'guanosine' named entity 'WHO' named entity 'RNA' named entity 'antiviral effect' named entity 'ZIKV' named entity 'Ebola' named entity 'virus replication' named entity 'protein' named entity 'lysozyme' named entity 'Fluorescent' named entity 'nucleotides' named entity 'epigenetic' named entity 'Filoviruses' named entity 'RNA' named entity 'guanosine diphosphate' named entity 'RNA' named entity 'biochemical' named entity 'genus' named entity 'RNA' named entity 'Methylation' named entity 'RIG-I' named entity 'RNA' named entity 'lysed' named entity 'Agilent' named entity 'RNAs' named entity 'Fluorescence polarization' named entity 'substrates'

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