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.
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TL;DR: It is shown that a promoter-associated RNA polymerase II molecule is transcriptionally engaged and has formed a nascent RNA chain, but is apparently arrested at that point and unable to penetrate further into the hsp70 gene without heat induction.
631 citations
TL;DR: An RNA molecule is described that catalyzes the type of polymerization needed for RNA replication, which uses nucleoside triphosphates and the coding information of an RNA template to extend an RNA primer by the successive addition of up to 14 nucleotides.
Abstract: The RNA world hypothesis regarding the early evolution of life relies on the premise that some RNA sequences can catalyze RNA replication. In support of this conjecture, we describe here an RNA molecule that catalyzes the type of polymerization needed for RNA replication. The ribozyme uses nucleoside triphosphates and the coding information of an RNA template to extend an RNA primer by the successive addition of up to 14 nucleotides-more than a complete turn of an RNA helix. Its polymerization activity is general in terms of the sequence and the length of the primer and template RNAs, provided that the 3' terminus of the primer pairs with the template. Its polymerization is also quite accurate: when primers extended by 11 nucleotides were cloned and sequenced, 1088 of 1100 sequenced nucleotides matched the template.
628 citations
TL;DR: It is shown that C. elegans eri-1 encodes an evolutionarily conserved protein with domains homologous to nucleic-acid-binding and exonuclease proteins that may normally function to limit the duration, cell-type specificity or endogenous functions of RNA interference.
Abstract: In many organisms, introducing double-stranded RNA (dsRNA) causes the degradation of messenger RNA that is homologous to the trigger dsRNA--a process known as RNA interference. The dsRNA is cleaved into short interfering RNAs (siRNAs), which hybridize to homologous mRNAs and induce their degradation. dsRNAs vary in their ability to trigger RNA interference: many mRNA-targeting dsRNAs show weak phenotypes, and nearly all mRNAs of the Caenorhabditis elegans nervous system are refractory to RNA interference. C. elegans eri-1 was identified in a genetic screen for mutants with enhanced sensitivity to dsRNAs. Here we show that eri-1 encodes an evolutionarily conserved protein with domains homologous to nucleic-acid-binding and exonuclease proteins. After exposure to dsRNA or siRNAs, animals with eri-1 mutations accumulate more siRNAs than do wild-type animals. C. elegans ERI-1 and its human orthologue degrade siRNAs in vitro. In the nematode worm, ERI-1 is predominantly cytoplasmic and is expressed most highly in the gonad and a subset of neurons, suggesting that ERI-1 siRNase activity suppresses RNA interference more intensely in these tissues. Thus, ERI-1 is a negative regulator that may normally function to limit the duration, cell-type specificity or endogenous functions of RNA interference.
626 citations
TL;DR: The molecular basis of SARS-CoV-2 RNA replication is examined by determining the cryo-EM structures of the stalled pre-/post- translocated polymerase complexes and the inhibition mechanisms of the triphosphate metabolite of remdesivir are investigated through structural and kinetic analyses.
617 citations
TL;DR: It is proposed that the holoenzyme is a form of RNA polymerase II readily recruited to promoters in vivo, a multi-subunit complex containing roughly equimolar amounts of RNA Polymerase II, a subset of general transcription factors, and SRB regulatory proteins.
Abstract: RNA POLYMERASE II requires multiple general transcription factors to initiate site-specific transcription1–3 These proteins can assemble in an ordered fashion onto promoter DNA in vitro2–8, and such ordered assembly may occur in vivo (Fig la) Some general transcription factors can interact with RNA polymerase II in the absence of DNA3,9–15, however, suggesting that RNA polymerase II may also assemble into a multi-component complex containing a subset of initiation factors before binding to promoter DNA (Fig Ib) Here we present evidence from the yeast Saccharo-myces cerevisiae for such an RNA polymerase II holoenzyme, a multi-subunit complex containing roughly equimolar amounts of RNA polymerase II, a subset of general transcription factors, and SRB regulatory proteins Transcription by this holoenzyme is stimulated by the activator protein GAL4-VP16, a feature not observed with purified RNA polymerase II and general transcription factors alone We propose that the holoenzyme is a form of RNA polymerase II readily recruited to promoters in vivo
616 citations