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Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
Published on: May 13, 2019
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Structure of the transcribing RNA polymerase II-Elongin complex
Ying Chen1,2, Goran Kokic1, Christian Dienemann1
1Department of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Nature Structural & Molecular Biology
|November 6, 2023
Summary
Elongin, a transcription factor, binds RNA polymerase II (Pol II) via its ELOA subunit. This interaction allosterically regulates Pol II’s active center, enhancing transcription elongation.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Elongin is a conserved heterotrimeric transcription elongation factor for RNA polymerase II (Pol II).
- Understanding Elongin's mechanism is crucial for deciphering gene transcription regulation.
Purpose of the Study:
- To elucidate the structural basis of Elongin's interaction with transcribing Pol II.
- To determine how Elongin stimulates RNA polymerase II transcription elongation.
Main Methods:
- Three cryo-electron microscopy (cryo-EM) structures of human Elongin bound to transcribing Pol II were determined.
- Structural analysis focused on the binding interfaces and conformational changes induced by Elongin.
Main Results:
- Elongin subunit ELOA binds the RPB2 subunit of Pol II, anchoring the ELOB-ELOC heterodimer.
- ELOA's 'latch' region induces a conformational change near the Pol II active center, crucial for elongation stimulation.
- Elongin binding is mutually exclusive with other elongation factors like the super elongation complex, PAF1 complex, and RTF1.
Conclusions:
- Elongin allosterically regulates Pol II activity through conformational changes induced by its latch region.
- This mechanism highlights a novel mode of transcription elongation control.
- Elongin's distinct binding site suggests specific roles in transcription regulation compared to other elongation factors.
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