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Related Concept Videos

Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

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...
Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

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...
Transcription Initiation01:47

Transcription Initiation

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...
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

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...
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

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...
Translesion DNA Polymerases02:10

Translesion DNA Polymerases

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.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...

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DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation
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T7 RNA polymerase functions in vitro without clustering.

Kieran Finan1, Joseph P Torella, Achillefs N Kapanidis

  • 1Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.

Plos One
|July 7, 2012
PubMed
Summary

Active phage T7 RNA polymerase (RNAP) does not appear to cluster in vitro. Further research is needed to determine if weak interactions or phage proteins mediate in vivo clustering of RNAP.

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Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Many nucleic acid polymerases form active clusters, termed 'polymerase factories'.
  • The clustering behavior of bacteriophage T7 RNA polymerase (RNAP) remains largely uncharacterized.

Purpose of the Study:

  • To investigate whether active bacteriophage T7 RNA polymerase (RNAP) forms clusters in vitro and in vivo.
  • To determine the interaction strength between T7 RNAP elongation complexes.

Main Methods:

  • Pulldown assays to assess protein interactions.
  • Fluorescence correlation spectroscopy (FCS) to quantify complex formation.
  • Chromosome conformation capture (3C) to analyze gene associations.

Main Results:

  • T7 RNAP elongation complexes exhibit no significant interaction in vitro (K(d) < 1 µM).
  • Chromosome conformation capture revealed no increased association of co-transcribed genes (100 kb apart) by T7 RNAP.

Conclusions:

  • Clustering of T7 RNAP, if it occurs in vivo, is not driven by strong direct interactions between elongation complexes.
  • Potential mechanisms for in vivo clustering include weak, transient interactions or mediation by phage-encoded proteins.