Structure of the transcribing RNA polymerase II–Elongin complex
2023 | journal article. A publication with affiliation to the University of Göttingen.
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- Authors
- Chen, Ying; Kokic, Goran; Dienemann, Christian; Dybkov, Olexandr; Urlaub, Henning; Cramer, Patrick
- Abstract
- Abstract Elongin is a heterotrimeric elongation factor for RNA polymerase (Pol) II transcription that is conserved among metazoa. Here, we report three cryo-EM structures of human Elongin bound to transcribing Pol II. The structures show that Elongin subunit ELOA binds the RPB2 side of Pol II and anchors the ELOB–ELOC subunit heterodimer. ELOA contains a ‘latch’ that binds between the end of the Pol II bridge helix and funnel helices, thereby inducing a conformational change near the polymerase active center. The latch is required for the elongation-stimulatory activity of Elongin, but not for Pol II binding, indicating that Elongin functions by allosterically regulating the conformational mobility of the polymerase active center. Elongin binding to Pol II is incompatible with association of the super elongation complex, PAF1 complex and RTF1, which also contain an elongation-stimulatory latch element.
- Issue Date
- 2023
- Journal
- Nature Structural & Molecular Biology
- Project
- SFB 1565: Molekulare Mechanismen und Vernetzung von Prozessen der Genexpression
SFB 1565 | P04: Analyse von Protein-RNA- und -DNA-Wechselwirkungen in Zellen durch Quervernetzungs-Massenspektrometrie
EXC 2067: Multiscale Bioimaging - Working Group
- RG Urlaub (Bioanalytik)
RG Cramer - ISSN
- 1545-9993
- eISSN
- 1545-9985
- Language
- English