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Related Concept Videos

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...
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...
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...
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...
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...
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...

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Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
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Published on: May 13, 2019

Yeast RNA polymerase II at 5 A resolution.

J Fu1, A L Gnatt, D A Bushnell

  • 1Department of Structural Biology, Stanford University School of Medicine, Fairchild Science Center, California 94305, USA.

Cell
|September 28, 1999
PubMed
Summary
This summary is machine-generated.

Researchers used X-ray diffraction to determine the structure of yeast RNA polymerase II. This revealed mobile protein domains acting as DNA and RNA clamps during transcription.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Yeast RNA polymerase II is crucial for gene transcription.
  • Understanding its structure is key to deciphering its function.

Purpose of the Study:

  • To determine the high-resolution structure of yeast RNA polymerase II.
  • To elucidate the functional roles of mobile protein domains in transcription.

Main Methods:

  • X-ray diffraction of an 18-heavy atom cluster derivative of yeast RNA polymerase II crystal.
  • Phase information obtained to 5 A resolution.
  • Comparison with electron crystallography data.

Main Results:

  • Significant phase information was obtained to 5 A resolution.
  • A 6 A electron density map closely matched a 16 A molecular envelope from electron crystallography, validating the phases.
  • Two mobile protein domains were identified: a downstream DNA clamp and a hinged RNA clamp enclosing the transcript.

Conclusions:

  • The study provides structural insights into yeast RNA polymerase II function.
  • Mobile protein domains play critical roles in DNA binding and RNA encapsulation during transcription.
  • The findings advance our understanding of the transcription elongation mechanism.