About: The Expanding Functions of Cellular Helicases: The Tombusvirus RNA Replication Enhancer Co-opts the Plant eIF4AIII-Like AtRH2 and the DDX5-Like AtRH5 DEAD-Box RNA Helicases to Promote Viral Asymmetric RNA Replication

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About: The Expanding Functions of Cellular Helicases: The Tombusvirus RNA Replication Enhancer Co-opts the Plant eIF4AIII-Like AtRH2 and the DDX5-Like AtRH5 DEAD-Box RNA Helicases to Promote Viral Asymmetric RNA Replication 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	The Expanding Functions of Cellular Helicases: The Tombusvirus RNA Replication Enhancer Co-opts the Plant eIF4AIII-Like AtRH2 and the DDX5-Like AtRH5 DEAD-Box RNA Helicases to Promote Viral Asymmetric RNA Replication
Creator	Kovalev, Nikolay Nagy, Peter
Source	PMC
abstract	Replication of plus-strand RNA viruses depends on recruited host factors that aid several critical steps during replication. Several of the co-opted host factors bind to the viral RNA, which plays multiple roles, including mRNA function, as an assembly platform for the viral replicase (VRC), template for RNA synthesis, and encapsidation during infection. It is likely that remodeling of the viral RNAs and RNA-protein complexes during the switch from one step to another requires RNA helicases. In this paper, we have discovered a second group of cellular RNA helicases, including the eIF4AIII-like yeast Fal1p and the DDX5-like Dbp3p and the orthologous plant AtRH2 and AtRH5 DEAD box helicases, which are co-opted by tombusviruses. Unlike the previously characterized DDX3-like AtRH20/Ded1p helicases that bind to the 3′ terminal promoter region in the viral minus-strand (−)RNA, the other class of eIF4AIII-like RNA helicases bind to a different cis-acting element, namely the 5′ proximal RIII(−) replication enhancer (REN) element in the TBSV (−)RNA. We show that the binding of AtRH2 and AtRH5 helicases to the TBSV (−)RNA could unwind the dsRNA structure within the RIII(−) REN. This unique characteristic allows the eIF4AIII-like helicases to perform novel pro-viral functions involving the RIII(−) REN in stimulation of plus-strand (+)RNA synthesis. We also show that AtRH2 and AtRH5 helicases are components of the tombusvirus VRCs based on co-purification experiments. We propose that eIF4AIII-like helicases destabilize dsRNA replication intermediate within the RIII(−) REN that promotes bringing the 5′ and 3′ terminal (−)RNA sequences in close vicinity via long-range RNA-RNA base pairing. This newly formed RNA structure promoted by eIF4AIII helicase together with AtRH20 helicase might facilitate the recycling of the viral replicases for multiple rounds of (+)-strand synthesis, thus resulting in asymmetrical viral replication.
has issue date	2014-04-17(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1004051
bibo:pmid	24743583
has license	cc-by
sha1sum (hex)	5534fcf5c7e7df182da3c253d2312cd5662259b8
schema:url	https://doi.org/10.1371/journal.ppat.1004051
resource representing a document's title	The Expanding Functions of Cellular Helicases: The Tombusvirus RNA Replication Enhancer Co-opts the Plant eIF4AIII-Like AtRH2 and the DDX5-Like AtRH5 DEAD-Box RNA Helicases to Promote Viral Asymmetric RNA Replication
has PubMed Central identifier	PMC3990711
has PubMed identifier	24743583
schema:publication	PLoS Pathog
resource representing a document's body	covid:5534fcf5c7e7df182da3c253d2312cd5662259b8#body_text
is schema:about of	named entity 'ASYMMETRIC' named entity 'factors' named entity 'DDX5' named entity 'replication' named entity 'replication' named entity 'promotes' named entity 'Replication' named entity 'Cellular' named entity 'DEAD-BOX RNA HELICASES' named entity 'LIKE' named entity 'ELEMENT' named entity 'VICINITY' covid:arg/5534fcf5c7e7df182da3c253d2312cd5662259b8 named entity 'CO-PURIFICATION' named entity 'BASED' named entity 'CLASS' named entity 'YEAST' named entity 'MRNA' named entity 'REMODELING' named entity 'EXPANDING' named entity 'FUNCTIONS' named entity 'RNA' named entity 'RNA VIRUSES' named entity 'RNAS' named entity 'MINUS' named entity 'PERFORM' named entity '282' named entity 'EXPERIMENTS' named entity 'NOVEL' named entity 'HELICASES' named entity 'HOST' named entity 'DEAD' named entity 'PLANT' named entity 'BASE PAIRING' named entity 'PLATFORM' named entity 'ALLOWS' named entity 'PROXIMAL' named entity 'ASSEMBLY' named entity 'EXPANDING' named entity 'STRUCTURE' named entity 'RNA HELICASES' named entity 'CELLULAR' named entity 'NEWLY' named entity 'ENCAPSIDATION' named entity 'PROTEIN COMPLEXES' named entity 'TEMPLATE' named entity 'CIS-ACTING ELEMENT' named entity 'REPLICASE' named entity 'INVOLVING' named entity 'PROMOTE' named entity 'EIF4AIII' named entity 'PLANT' named entity 'CELLULAR' named entity 'UNIQUE' named entity 'ROLES' named entity 'PREVIOUSLY' named entity 'TOMBUSVIRUS' named entity 'SECOND' named entity 'STEPS' named entity 'REGION' named entity 'REN' named entity 'RECYCLING' named entity 'BOX' named entity 'CHARACTERISTIC' named entity 'RNA STRUCTURE' named entity '10%' named entity 'TBSV' named entity 'ONE STEP' named entity 'LIKELY' named entity 'LONG' named entity 'EIF4AIII' named entity 'CITATION' named entity 'RANGE' named entity 'ASYMMETRIC' named entity 'SWITCH' named entity 'FUNCTION' named entity 'DDX3' named entity 'FUNCTIONS' named entity 'SEQUENCES' named entity 'RESULTING IN'

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