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Related Concept Videos

Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

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RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
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The Replisome03:01

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DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
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Transcription Initiation01:47

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Initiation is the first step of transcription in eukaryotes. Prokaryotic RNA Polymerase (RNAP) can bind to the template DNA and start transcribing. On the other hand, transcription in eukaryotes requires additional proteins, called transcription factors, to first bind to the promoter region in the DNA template. This binding helps recruit the specific RNAP that can assemble on the DNA and start transcription.
The promoters and enhancers and their accessory proteins allow tight regulation of...
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Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

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Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
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Related Experiment Video

Updated: Dec 18, 2025

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method
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Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method

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Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase.

Quan Wang1, Jiqin Wu2, Haofeng Wang3

  • 1Shanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, China.

Cell
|June 12, 2020
PubMed
Summary

Understanding SARS-CoV-2 RNA replication is key for COVID-19 treatment. This study reveals the structure of the viral polymerase complex and how remdesivir inhibits it, offering insights into coronavirus replication machinery.

Keywords:
2019-nCoVCOVID-19RdRPSARS-CoV-2favipiravirnsp12nsp8polymeraseremdesivirvirus

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Direct Restart of a Replication Fork Stalled by a Head-On RNA Polymerase
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Area of Science:

  • Structural Biology
  • Virology
  • Biochemistry

Background:

  • Nucleotide analog inhibitors like remdesivir show promise for COVID-19 treatment.
  • The precise drug interactions with SARS-CoV-2 RNA-dependent RNA polymerase (nsp12) remain incompletely understood.

Purpose of the Study:

  • To elucidate the molecular mechanisms of SARS-CoV-2 RNA replication.
  • To investigate the structural basis of inhibition by remdesivir.

Main Methods:

  • Determined cryo-electron microscopy (cryo-EM) structures of stalled SARS-CoV-2 polymerase complexes (pre- and post-translocated).
  • Performed structural and kinetic analyses of remdesivir's triphosphate metabolite.
  • Proposed a transition model for the primase to polymerase complex.

Main Results:

  • Observed significant structural rearrangements in nsp12 and its co-factors (nsp7, nsp8) upon nucleic acid binding.
  • Identified conserved residues in nsp12 crucial for nucleotide incorporation.
  • Characterized the inhibition mechanism of remdesivir.

Conclusions:

  • Structural insights into the SARS-CoV-2 polymerase complex provide a basis for understanding viral RNA replication.
  • The findings offer clues for developing effective coronavirus transcription and replication inhibitors.