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Related Concept Videos

Proofreading01:31

Proofreading

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Synthesis of new DNA molecules is carried out by the enzyme DNA polymerase, which adds nucleotides on the daughter strand complementary to the template DNA strand. DNA polymerase has a higher affinity to add the correct base and ensures fidelity during DNA replication. Furthermore,  it exhibits proofreading activity during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.
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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.
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Translesion DNA Polymerases02:10

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Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
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Eukaryotic RNA Polymerases00:58

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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.
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Related Experiment Video

Updated: Mar 8, 2026

Isolation of Fidelity Variants of RNA Viruses and Characterization of Virus Mutation Frequency
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Isolation of Fidelity Variants of RNA Viruses and Characterization of Virus Mutation Frequency

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Picornaviral polymerase structure, function, and fidelity modulation.

Olve B Peersen1

  • 1Department of Biochemistry & Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, United States.

Virus Research
|February 7, 2017
PubMed
Summary

Picornaviruses use a unique RNA-dependent RNA polymerase (3Dpol) for genome replication. This enzyme

Keywords:
PicornavirusPolymerasePositive strand RNA virusRNA-dependent RNA polymeraseStructure

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Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Picornaviruses replicate genomes using a viral RNA-dependent RNA polymerase (3Dpol).
  • Understanding 3Dpol structure and function has advanced significantly over the past decade.

Purpose of the Study:

  • To review current knowledge of picornaviral polymerase structure.
  • To elucidate how 3Dpol interacts with RNA and viral proteins.

Main Methods:

  • Literature review of studies on picornaviral polymerase.
  • Analysis of structural and functional data for 3Dpol.

Main Results:

  • Picornaviral 3Dpol possesses a novel active site closure mechanism.
  • This mechanism allows fine-tuning of replication fidelity and quasispecies distributions.
  • 3Dpol forms stable and processive elongation complexes through interactions with RNA and viral proteins.

Conclusions:

  • Picornaviral RNA-dependent RNA polymerases (RdRPs) are among the smallest viral polymerases.
  • The fundamental catalytic mechanism of picornaviral RdRPs is likely conserved across positive-strand RNA viruses.