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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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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.
The promoters and enhancers and their accessory proteins allow tight regulation of...
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Transcription Attenuation in Prokaryotes02:42

Transcription Attenuation in Prokaryotes

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Transcriptional attenuation occurs when RNA transcription is prematurely terminated due to the formation of a terminator mRNA hairpin structure.  Bacteria use these hairpins to regulate the transcription process and control the synthesis of several amino acids including histidine, lysine, threonine, and phenylalanine. Transcription attenuation takes place in the non-coding regions of mRNA.
There are several different mechanisms used to attenuate transcription. In ribosome mediated...
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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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RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

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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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Termination of Translation01:44

Termination of Translation

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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Related Experiment Video

Updated: Jun 29, 2025

Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on TRO Approach
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Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on TRO Approach

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Structural basis of Integrator-dependent RNA polymerase II termination.

Isaac Fianu1, Moritz Ochmann2, James L Walshe2

  • 1Department of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany. isaac.fianu@mpinat.mpg.de.

Nature
|April 3, 2024
PubMed
Summary

The Integrator complex terminates RNA polymerase II (Pol II) transcription. Structural studies reveal how Integrator removes Pol II from DNA and prevents its re-binding, clarifying transcription termination mechanisms.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Gene Regulation

Background:

  • The Integrator complex is known to bind paused elongation complexes and cleave nascent RNA during transcription termination.
  • The mechanism by which Integrator removes RNA polymerase II (Pol II) from the DNA template after transcription has remained unclear.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying RNA polymerase II transcription termination by the Integrator complex.
  • To understand the role of different Integrator subunits and associated factors in the termination process.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structures of the Integrator-PP2A complex in multiple functional states.
  • Analysis of pre-termination, post-termination, and inactive complex structures.

Main Results:

  • A novel INTS10-INTS13-INTS14-INTS15 module was identified in the pre-termination complex, potentially involved in opening the DSIF DNA clamp.
  • The INTS3 subunit and SOSS factors were shown to prevent Pol II re-binding in the post-termination complex.
  • The INTS6 subunit was found to block the PP2A phosphatase active site in the inactive complex.

Conclusions:

  • A three-step model for Integrator-mediated Pol II transcription termination is proposed, involving significant structural rearrangements.
  • These findings provide atomic-level insights into the regulation of transcription termination by the Integrator complex.