About: Human Enterovirus Nonstructural Protein 2C(ATPase) Functions as Both an RNA Helicase and ATP-Independent RNA Chaperone

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About: Human Enterovirus Nonstructural Protein 2C(ATPase) Functions as Both an RNA Helicase and ATP-Independent RNA Chaperone 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 Enterovirus Nonstructural Protein 2C(ATPase) Functions as Both an RNA Helicase and ATP-Independent RNA Chaperone
Creator	Qin, Cheng-Feng Yang, Jie Yin, Lei Wu, Wenzhe Shu, Ting Zhou, Xi Hu, Yuanyang Qiu, Yang Xia, Hongjie Zhao, Xiaolu Sun, Xianlin Wang, Guang-Chuan Wang, Peipei
topic	covid:f58cfab11be3906401550ffe0ba6e444d1056853#this
Source	Medline; PMC
abstract	RNA helicases and chaperones are the two major classes of RNA remodeling proteins, which function to remodel RNA structures and/or RNA-protein interactions, and are required for all aspects of RNA metabolism. Although some virus-encoded RNA helicases/chaperones have been predicted or identified, their RNA remodeling activities in vitro and functions in the viral life cycle remain largely elusive. Enteroviruses are a large group of positive-stranded RNA viruses in the Picornaviridae family, which includes numerous important human pathogens. Herein, we report that the nonstructural protein 2C(ATPase) of enterovirus 71 (EV71), which is the major causative pathogen of hand-foot-and-mouth disease and has been regarded as the most important neurotropic enterovirus after poliovirus eradication, functions not only as an RNA helicase that 3′-to-5′ unwinds RNA helices in an adenosine triphosphate (ATP)-dependent manner, but also as an RNA chaperone that destabilizes helices bidirectionally and facilitates strand annealing and complex RNA structure formation independently of ATP. We also determined that the helicase activity is based on the EV71 2C(ATPase) middle domain, whereas the C-terminus is indispensable for its RNA chaperoning activity. By promoting RNA template recycling, 2C(ATPase) facilitated EV71 RNA synthesis in vitro; when 2C(ATPase) helicase activity was impaired, EV71 RNA replication and virion production were mostly abolished in cells, indicating that 2C(ATPase)-mediated RNA remodeling plays a critical role in the enteroviral life cycle. Furthermore, the RNA helicase and chaperoning activities of 2C(ATPase) are also conserved in coxsackie A virus 16 (CAV16), another important enterovirus. Altogether, our findings are the first to demonstrate the RNA helicase and chaperoning activities associated with enterovirus 2C(ATPase), and our study provides both in vitro and cellular evidence for their potential roles during viral RNA replication. These findings increase our understanding of enteroviruses and the two types of RNA remodeling activities.
has issue date	2015-07-28(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1005067
bibo:pmid	26218680
has license	cc-by
sha1sum (hex)	f58cfab11be3906401550ffe0ba6e444d1056853
schema:url	https://doi.org/10.1371/journal.ppat.1005067
resource representing a document's title	Human Enterovirus Nonstructural Protein 2C(ATPase) Functions as Both an RNA Helicase and ATP-Independent RNA Chaperone
has PubMed Central identifier	PMC4517893
has PubMed identifier	26218680
schema:publication	PLoS Pathog
resource representing a document's body	covid:f58cfab11be3906401550ffe0ba6e444d1056853#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/f58cfab11be3906401550ffe0ba6e444d1056853
is schema:about of	named entity 'ENTEROVIRUS 71' named entity 'PROTEINS' named entity 'ABOLISHED' named entity 'CONSERVED' named entity 'ROLES' named entity 'DETERMINED' named entity 'FINDINGS' named entity 'NEUROTROPIC' named entity 'INDICATING' named entity 'COXSACKIE A VIRUS' named entity 'STUDY' named entity 'HUMAN' named entity 'ATPASE' named entity 'STRAND' named entity 'ATP' named entity 'IMPORTANT' named entity 'IDENTIFIED' named entity 'POTENTIAL' named entity 'BASED' named entity 'LARGE' named entity 'TYPES' named entity 'COMPLEX' named entity 'POLIOVIRUS' named entity 'PROTEIN ' named entity 'IN VITRO' named entity 'CRITICAL' named entity 'CLASSES' named entity 'RNA HELICASE' named entity 'DOMAIN' named entity 'PROMOTING' named entity 'HELICES' named entity 'RNA SYNTHESIS' named entity 'VIRUS' named entity 'VIRAL RNA' named entity 'LIFE CYCLE' named entity 'ROLE' named entity 'GROUP' named entity 'HUMAN ENTEROVIRUS' named entity 'helicase' named entity 'remodeling' named entity 'pathogen' named entity 'replication' named entity 'RNA' named entity 'major' named entity 'activity' named entity 'Chaperone' named entity 'RNA' named entity 'ASSOCIATED WITH' named entity 'PROTEIN INTERACTIONS' named entity 'INCREASE' named entity 'ITS' named entity 'RNA REPLICATION' named entity 'BUT' named entity 'THEIR' named entity 'CELLULAR' named entity 'RNA HELICASES' named entity 'ACTIVITIES' named entity 'HAND-FOOT-AND-MOUTH DISEASE' named entity 'STRUCTURES' named entity 'RNA STRUCTURE' named entity 'LARGELY' named entity 'RNA' named entity 'DEPENDENT' named entity 'MIDDLE' named entity 'PROVIDES' named entity 'RNA CHAPERONE' named entity 'PROTEIN '

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