Structure of the transcribing RNA polymerase II–Elongin complex

Chen, Ying; Kokic, Goran; Dienemann, Christian; Dybkov, Olexandr; Urlaub, Henning; Cramer, Patrick

doi:10.1038/s41594-023-01138-w

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Structure of the transcribing RNA polymerase II–Elongin complex

MPS-Authors

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Chen, Ying
Department of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Kokic, Goran
Department of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Dienemann, Christian
Department of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Dybkov, Olexandr
Research Group of Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Urlaub, Henning
Research Group of Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Cramer, Patrick
Department of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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s41594-023-01138-w.pdf
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引用

Chen, Y., Kokic, G., Dienemann, C., Dybkov, O., Urlaub, H., & Cramer, P. (2023). Structure of the transcribing RNA polymerase II–Elongin complex. Nature Structural & Molecular Biology, 30, 1925-1935. doi:10.1038/s41594-023-01138-w.

引用: https://hdl.handle.net/21.11116/0000-000D-EAA6-0

要旨

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.