Topic
RNA-dependent RNA polymerase
About: RNA-dependent RNA polymerase is a research topic. Over the lifetime, 13904 publications have been published within this topic receiving 767954 citations. The topic is also known as: RdRp & RNA replicase.
Papers published on a yearly basis
Papers
More filters
TL;DR: It is found that NS5A has the capacity to bind to the 3′-ends of HCV plus and minus strand RNAs, and this protein defines a new functional target for development of agents to treat HCV infection and a new structural class of RNA-binding proteins.
267 citations
TL;DR: Cells producing Rous sarcoma virus contain virus-specific ribonucleic acid (RNA) which can be identified by hybridization to single-stranded deoxyribonucleics acid (DNA) synthesized with RNA-directed DNA polymerase, and the hybrids formed have a high order of thermal stability.
Abstract: Cells producing Rous sarcoma virus contain virus-specific ribonucleic acid (RNA) which can be identified by hybridization to single-stranded deoxyribonucleic acid (DNA) synthesized with RNA-directed DNA polymerase. Hybridization was detected by either fractionation on hydroxyapatite or hydrolysis with single strand-specific nucleases. Similar results were obtained with both procedures. The hybrids formed between enzymatically synthesized DNA and viral RNA have a high order of thermal stability, with only minor evidence of mismatched nucleotide sequences. Virus-specific RNA is present in both nuclei and cytoplasm of infected cells. This RNA is remarkably heterogeneous in size, including molecules which are probably restricted to the nucleus and which sediment in their native state more rapidly than the viral genome. The nature of the RNA found in cytoplasmic fractions varies from preparation to preparation, but heterogeneous RNA (ca. 4-50S), smaller than the viral genome, is always present in substantial amounts.
267 citations
TL;DR: The results suggest that the nucleoprotein binds to the vRNA backbone without apparent sequence specificity, exposing the bases to the outside and melting all secondary structure, and the viral polymerase may transcribe the RNA without the need for dissociating theucleoprotein and without being stopped by RNA secondary structure.
Abstract: The influenza virus genome consists of eight segments of negative-sense RNA, i.e. the viral (v) RNA forms the template for the mRNA. Each segment is encapsidated by the viral nucleoprotein to form a ribonucleoprotein (RNP) particle and each RNP carries its own polymerase complex. We studied the interaction of purified nucleoprotein with RNA in vitro, by using a variety of enzymatic and chemical probes for RNA conformation. Our results suggest that the nucleoprotein binds to the vRNA backbone without apparent sequence specificity, exposing the bases to the outside and melting all secondary structure. In this way, the viral polymerase may transcribe the RNA without the need for dissociating the nucleoprotein and without being stopped by RNA secondary structure, and the viral RNPs are ready to start transcription as soon as they enter the host cell.
266 citations
TL;DR: It is demonstrated that halting at such special sites does not “freeze” RNA polymerase at one location but induces it to leave its initial position and to slide backward along the DNA and the RNA without degrading the transcript.
266 citations
TL;DR: A model for promoter structure and function is put forth at two independent bacteriophage T7 early promoters and the nucleotide sequence of each promoter fragment and the sequence of the mRNA coded by each fragment are presented.
265 citations