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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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RNA Polymerase II Accessory Proteins02:36

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Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
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Transcription Initiation01:47

Transcription Initiation

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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.
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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.
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Bacterial Transcription01:53

Bacterial Transcription

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RNA polymerase (RNAP) carries out DNA-dependent RNA synthesis in both bacteria and eukaryotes. Bacteria do not have a membrane-bound nucleus. So, transcription and translation occur simultaneously, on the same DNA template.
Transcription can be divided into three main stages, each involving distinct DNA sequences to guide the polymerase. These are:
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The Eukaryotic Promoter Region02:40

The Eukaryotic Promoter Region

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The eukaryotic promoter region is a segment of DNA located upstream of a gene. It contains an RNA polymerase binding site, a transcription start site, and several cis-regulatory sequences.  The proximal promoter region is located in the vicinity of the gene and has cis-regulatory sequences and the core promoter. The core promoter is the binding site for RNA polymerase and is usually located between -35 and +35 nucleotides from the transcription start site. The distal promoter regions are...
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High-throughput Purification of Affinity-tagged Recombinant Proteins
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Expression of RNA polymerase I catalytic core is influenced by RPA12.

Brittany L Ford1,2, Ting Wei2, Hester Liu3

  • 1Drug Research Program, Faculty of Pharmacy, University of Helsinki, Helsinki, Finland.

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|May 11, 2023
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Summary

RNA Polymerase I (Pol I) subunit RPA12 affects basal expression of RPA194 in cancer cells but does not influence drug-induced degradation. This finding clarifies RPA12

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Area of Science:

  • Molecular Biology
  • Cancer Therapeutics
  • Biochemistry

Background:

  • RNA Polymerase I (Pol I) is crucial for ribosome biogenesis and is hyperactivated in cancers, making it a therapeutic target.
  • The catalytic core of Pol I includes subunits RPA194, RPA135, and RPA12, with RPA12 involved in RNA cleavage and transcription.
  • Understanding the regulatory roles of Pol I subunits is essential for developing targeted cancer therapies.

Purpose of the Study:

  • To investigate the influence of subunit RPA12 on the regulation of RPA194 in human cancer cells.
  • To determine if RPA12 affects the basal expression and drug-induced turnover of RPA194.

Main Methods:

  • Utilized the small-molecule Pol I inhibitor BMH-21 to study Pol I activity and subunit degradation.
  • Employed gene silencing techniques (RPA12 knockdown) to assess the impact on Pol I subunits.
  • Analyzed the expression, localization, and chromatin engagement of Pol I subunits (RPA194, RPA135) and Pol I transcription.

Main Results:

  • Silencing RPA12 altered the expression and localization of RPA194 and RPA135 but did not disrupt the RPA194-RPA135 core complex.
  • Pol I transcription and chromatin engagement remained unaffected by RPA12 knockdown.
  • BMH-21-induced degradation of RPA194 was independent of RPA12, indicating RPA12 regulates basal expression, not drug-induced turnover.

Conclusions:

  • RPA12 plays a role in the basal expression and localization of Pol I subunits RPA194 and RPA135.
  • RPA12 is not essential for the maintenance of the Pol I core complex or its transcriptional activity.
  • RPA12 does not mediate the BMH-21-induced degradation of RPA194, highlighting distinct regulatory mechanisms.