Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-3-25
pubmed:abstractText
The initiation of enteroviral positive-strand RNA synthesis requires the presence of a functional ribonucleoprotein complex containing a cloverleaf-like RNA secondary structure at the 5' end of the viral genome. Other components of the ribonucleoprotein complex are the viral 3CD proteinase (the precursor protein of the 3C proteinase and the 3D polymerase), the viral 3AB protein and the cellular poly(rC)-binding protein 2. For a molecular characterization of the RNA-binding properties of the enteroviral proteinase, the 3C proteinase of coxsackievirus B3 (CVB3) was bacterially expressed and purified. The recombinant protein is proteolytically active and forms a stable complex with in vitro-transcribed cloverleaf RNA of CVB3. The formation of stable complexes is also demonstrated with cloverleaf RNA of poliovirus (PV) 1, the first cloverleaf of bovine enterovirus (BEV) 1, and human rhinovirus (HRV) 2 but not with cloverleaf RNA of HRV14 and the second cloverleaf of BEV1. The apparent dissociation constants of the protein:RNA complexes range from approx. 1.7 to 4.6 microM. An electrophoretic mobility shift assay with subdomain D of the CVB3 cloverleaf demonstrates that this RNA is sufficient to bind the CVB3 3C proteinase. Binding assays using mutated versions of CVB3 and HRV14 cloverleaf RNAs suggest that the presence of structural features rather than a defined sequence motif of loop D are important for 3C proteinase-RNA interaction.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-10500114, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-10501480, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-11162821, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-11434774, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-1326654, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-1326828, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-1409538, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-1691929, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-2153227, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-2170027, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-2827387, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-2846872, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-334279, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-7745714, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-7782313, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-7908267, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-7929441, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-8039507, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-8245010, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-8253083, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-8641454, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-8672468, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-8837877, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-8855318, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-9056766, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-9123881, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-9129643, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-9257647, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-9326487, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-9498619, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-9799245, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-9847378, http://linkedlifedata.com/resource/pubmed/commentcorrection/11911365-993212
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1355-8382
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
188-201
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:11911365-Base Sequence, pubmed-meshheading:11911365-Binding Sites, pubmed-meshheading:11911365-Cloning, Molecular, pubmed-meshheading:11911365-Cysteine Endopeptidases, pubmed-meshheading:11911365-DNA, Complementary, pubmed-meshheading:11911365-DNA Primers, pubmed-meshheading:11911365-DNA-Binding Proteins, pubmed-meshheading:11911365-Enterovirus, pubmed-meshheading:11911365-Enterovirus B, Human, pubmed-meshheading:11911365-Heterogeneous-Nuclear Ribonucleoproteins, pubmed-meshheading:11911365-Humans, pubmed-meshheading:11911365-Kinetics, pubmed-meshheading:11911365-Molecular Sequence Data, pubmed-meshheading:11911365-Nucleic Acid Conformation, pubmed-meshheading:11911365-RNA, Viral, pubmed-meshheading:11911365-RNA-Binding Proteins, pubmed-meshheading:11911365-Recombinant Proteins, pubmed-meshheading:11911365-Restriction Mapping, pubmed-meshheading:11911365-Transcription, Genetic, pubmed-meshheading:11911365-Transcription Factors, pubmed-meshheading:11911365-Viral Proteins
pubmed:year
2002
pubmed:articleTitle
Determinants of the recognition of enteroviral cloverleaf RNA by coxsackievirus B3 proteinase 3C.
pubmed:affiliation
Institut für Virologie, Klinikum der Friedrich-Schiller-Universität, Jena, Germany. i6zero@rz.uni-jena.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't