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Updated: May 9, 2026
10:59
Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
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
Summary
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.
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.
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