Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2009-2-13
pubmed:abstractText
A phylogenetically conserved RNA structure within the open reading frame of poliovirus and other group C enteroviruses functions as a competitive inhibitor of the antiviral endoribonuclease RNase L. Hence, we call this viral RNA the RNase L competitive inhibitor RNA (RNase L ciRNA). In this investigation we used phylogenetic information, RNA structure prediction software, site-directed mutagenesis, and RNase L activity assays to identify functionally important sequences and structures of the RNase L ciRNA. A putative loop E motif is phylogenetically conserved in the RNA structure and mutations of nucleotides within the putative loop E motif destroyed the ability of the RNA molecule to inhibit RNase L. A putative H-H kissing loop interaction is phylogenetically conserved in the RNA structure and covariant polymorphisms that maintain the Watson-Crick complementarity required for the kissing interaction provide evidence of its importance. Compensatory mutations that disrupted and then restored the putative kissing interaction confirm that it contributes to the ability of the viral RNA to inhibit RNase L. RNase L was activated late during the course of poliovirus replication in HeLa cells, as virus replication and assembly neared completion. We conclude that a putative loop E motif and an H-H kissing loop interaction are key features of the group C enterovirus RNA associated with the inhibition of RNase L.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1555-8584
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
263-72
pubmed:dateRevised
2010-12-3
pubmed:meshHeading
pubmed:articleTitle
A putative loop E motif and an H-H kissing loop interaction are conserved and functional features in a group C enterovirus RNA that inhibits ribonuclease L.
pubmed:affiliation
Department of Microbiology, University of Colorado Denver, School of Medicine, Aurora, Colorado 80045, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural