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RNA-dependent RNA polymerase of hepatitis C virus binds to its coding region RNA stem-loop structure, 5BSL3.2, and its negative strand.

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TLDR
It is shown that NS5B binds to the complementary strand of 5BSL3.2.2N, indicating the involvement of the RNA stem-loop structure of the negative strand in the replication process, and suggesting the importance of theRNA element in the polymerization by RdRp.
Abstract
The hepatitis C virus NS5B RNA-dependent RNA polymerase (RdRp) is a key enzyme involved in viral replication. Interaction between NS5B RdRp and the viral RNA sequence is likely to be an important step in viral RNA replication. The C-terminal half of the NS5B-coding sequence, which contains the important cis-acting replication element, has been identified as an NS5B-binding sequence. In the present study, we confirm the specific binding of NS5B to one of the RNA stem–loop structures in the region, 5BSL3.2. In addition, we show that NS5B binds to the complementary strand of 5BSL3.2 (5BSL3.2N). The bulge structure of 5BSL3.2N was shown to be indispensable for tight binding to NS5B. In vitro RdRp activity was inhibited by 5BSL3.2N, indicating the importance of the RNA element in the polymerization by RdRp. These results suggest the involvement of the RNA stem–loop structure of the negative strand in the replication process.

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Citations
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End-to-end crosstalk within the hepatitis C virus genome mediates the conformational switch of the 3′X-tail region

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Replication enhancer elements within the open reading frame of tick-borne encephalitis virus and their evolution within the Flavivirus genus

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RNA Aptamers as Molecular Tools to Study the Functionality of the Hepatitis C Virus CRE Region

TL;DR: Functional characterization of a set of aptamers targeting the cis-acting replication element (CRE) of the HCV genome, an essential partner for viral replication and also involved in the regulation of protein synthesis, confirms the potential of the CRE as an anti-HCV target and support the use ofaptamers as molecular tools for investigating the functionality of RNA domains in viral genomes.
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Structure-function relationship in viral RNA genomes: The case of hepatitis C virus

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In vitro selection of the 3'-untranslated regions of the human liver mRNA that bind to the HCV nonstructural protein 5B.

TL;DR: It was demonstrated that both of the mRNA molecules bind to NS5B in the cytoplasm by means of IP-RT-PCR, suggesting these RNA molecules are regulated in vivo by NS5 B.
References
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Journal ArticleDOI

Mfold web server for nucleic acid folding and hybridization prediction

TL;DR: The objective of this web server is to provide easy access to RNA and DNA folding and hybridization software to the scientific community at large by making use of universally available web GUIs (Graphical User Interfaces).
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Classification of hepatitis C virus into six major genotypes and a series of subtypes by phylogenetic analysis of the NS-5 region

TL;DR: A new nomenclature for HCV variants is proposed in this communication that reflects the two-tiered nature of sequence differences between different viral isolates and describes criteria that would enable new variants to be assigned within the classification as they are discovered.
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Rapid evolution of RNA genomes

TL;DR: RNA viruses show high mutation frequencies partly because of a lack of the proofreading enzymes that assure fidelity of DNA replication, and high rates of replication reflected in rates of RNA genome evolution which can be more than a millionfold greater than the rates of the DNA chromosome evolution of their hosts.
Journal ArticleDOI

Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus.

TL;DR: Experimental evidence that an RNA‐dependent RNA polymerase is encoded by HCV and that this enzymatic activity is the function of the 65 kDa non‐structural protein 5B (NS5B) is presented, representing a first important step towards a better understanding of the life cycle of the HCV.
Journal ArticleDOI

Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus supergroups

TL;DR: It is reported here that HCV shares an even greater degree of protein sequence similarity with members of the pestivirus group (i.e., bovine viral diarrhea virus and hog cholera virus), which are thought to be distantly related to the flaviviruses.
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