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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...
Bacterial RNA Polymerase00:43

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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.
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...
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.
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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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Multiple active centers of multi-subunit RNA polymerases.

Yulia Yuzenkova1, Mohammad Roghanian, Nikolay Zenkin

  • 1Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.

Transcription
|July 10, 2012
PubMed
Summary

The RNA polymerase active center has two key modules: the Mg(2+) module and the flexible Trigger Loop (TL). The TL module can be swapped with others, altering the enzyme's catalytic abilities.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Multi-subunit RNA polymerase is crucial for gene transcription.
  • Its active center comprises a Mg(2+) module and a flexible Trigger Loop (TL) module.
  • The TL module's unique adaptability influences catalytic properties.

Purpose of the Study:

  • To investigate the structural and functional significance of the Trigger Loop module in RNA polymerase.
  • To explore the impact of substituting the TL module on the enzyme's catalytic activity.
  • To understand the modular nature of the RNA polymerase active center.

Main Methods:

  • Structural analysis of RNA polymerase active center.
  • Biochemical assays to measure catalytic activity.
  • Site-directed mutagenesis to substitute the Trigger Loop module.

Main Results:

  • The Mg(2+) module and TL module are distinct functional units within the active center.
  • Substitution of the TL module with alternative modules demonstrably alters catalytic properties.
  • The flexibility of the TL module is key to its adaptable role.

Conclusions:

  • The RNA polymerase active center is modular, with the TL module offering a point for functional diversification.
  • Alternative modules can be integrated to modulate enzyme catalysis.
  • This modularity provides a mechanism for regulating transcription.