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Related Concept Videos

RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

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...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

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...
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...
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...
Chromatin Structure Regulates pre-mRNA Processing02:41

Chromatin Structure Regulates pre-mRNA Processing

In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
The chromatin structure, especially...

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Updated: May 19, 2026

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
10:59

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

Polycomb repressive complex 1 (PRC1) disassembles RNA polymerase II preinitiation complexes.

Lynn Lehmann1, Roberto Ferrari, Ajay A Vashisht

  • 1Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095-1737, USA.

The Journal of Biological Chemistry
|August 23, 2012
PubMed
Summary
This summary is machine-generated.

Polycomb repressive complex 1 (PRC1) silences genes by blocking Mediator recruitment during transcription initiation. This mechanism spares Tata Binding Protein (TBP) and TFIID, revealing how PRC1 inactivates gene expression.

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Last Updated: May 19, 2026

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Promoter Capture Hi-C: High-resolution, Genome-wide Profiling of Promoter Interactions
10:16

Promoter Capture Hi-C: High-resolution, Genome-wide Profiling of Promoter Interactions

Published on: June 28, 2018

Area of Science:

  • Epigenetics
  • Molecular Biology
  • Gene Regulation

Background:

  • Polycomb repressive complex 1 (PRC1) is crucial for genome-wide gene silencing.
  • The precise biochemical mechanisms by which PRC1 inhibits transcription remain largely unknown.

Purpose of the Study:

  • To investigate how recombinant PRC1 inhibits the assembly of the RNA polymerase II preinitiation complex (PIC).
  • To elucidate the specific molecular interactions underlying PRC1-mediated transcriptional silencing.

Main Methods:

  • In vitro transcription assays using immobilized H3K27-methylated chromatin templates.
  • Biochemical experiments with purified PRC1, TFIID, and Mediator.
  • Analysis of published genome-wide datasets from mouse embryonic stem cells.

Main Results:

  • Recombinant PRC1 inhibited transcription by blocking Mediator recruitment to PICs.
  • PRC1 did not significantly affect activator binding or TFIID recruitment.
  • Tata Binding Protein (TBP) showed resistance to PRC1-mediated eviction.
  • Genome-wide data showed co-enrichment of Ring1b (PRC1 subunit) and TBP at developmental genes.

Conclusions:

  • PRC1 silences transcription by interfering with Mediator recruitment, a key step in PIC assembly.
  • PRC1 leaves TBP and TFIID largely intact, indicating a specific inhibitory mechanism.
  • PRC1 and TFIID may co-occupy poised developmental genes, suggesting a role in transcriptional memory.