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Structural basis of RNA polymerase II backtracking, arrest and reactivation

Author

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  • Alan C. M. Cheung

    (Center for Integrated Protein Science Munich, Ludwig-Maximilians-Universität München, Feodor-Lynen-Str. 25)

  • Patrick Cramer

    (Center for Integrated Protein Science Munich, Ludwig-Maximilians-Universität München, Feodor-Lynen-Str. 25)

Abstract

The to and fro of RNA polymerase RNA polymerase II (RNA pol II) moves forwards along the DNA strand during gene transcription, synthesizing messenger RNA as it goes. It can also move backwards and stall — a useful property for regulatory purposes or if it hits an obstacle such as a nucleosome. This arrested state is reactivated by transcription factor IIS (TFIIS). Now, the crystal structure of a backtracked yeast RNA pol II complex containing observable backtracked RNA has been determined at 3.3 Å resolution, as well as the structure of a backtracked complex containing TFIIS. The structures reveal possible mechanisms of transcriptional stalling and transcription reactivation.

Suggested Citation

  • Alan C. M. Cheung & Patrick Cramer, 2011. "Structural basis of RNA polymerase II backtracking, arrest and reactivation," Nature, Nature, vol. 471(7337), pages 249-253, March.
    • Handle: RePEc:nat:nature:v:471:y:2011:i:7337:d:10.1038_nature09785
    DOI: 10.1038/nature09785
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    Cited by:

    1. Lisa-Marie Appel & Vedran Franke & Melania Bruno & Irina Grishkovskaya & Aiste Kasiliauskaite & Tanja Kaufmann & Ursula E. Schoeberl & Martin G. Puchinger & Sebastian Kostrhon & Carmen Ebenwaldner & M, 2021. "PHF3 regulates neuronal gene expression through the Pol II CTD reader domain SPOC," Nature Communications, Nature, vol. 12(1), pages 1-24, December.
    2. Simona Pilotto & Michal Sýkora & Gwenny Cackett & Christopher Dulson & Finn Werner, 2024. "Structure of the recombinant RNA polymerase from African Swine Fever Virus," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    3. Lisa-Marie Appel & Vedran Franke & Johannes Benedum & Irina Grishkovskaya & Xué Strobl & Anton Polyansky & Gregor Ammann & Sebastian Platzer & Andrea Neudolt & Anna Wunder & Lena Walch & Stefanie Kais, 2023. "The SPOC domain is a phosphoserine binding module that bridges transcription machinery with co- and post-transcriptional regulators," Nature Communications, Nature, vol. 14(1), pages 1-22, December.
    4. Phong Quoc Nguyen & Sonia Huecas & Amna Asif-Laidin & Adrián Plaza-Pegueroles & Beatrice Capuzzi & Noé Palmic & Christine Conesa & Joël Acker & Juan Reguera & Pascale Lesage & Carlos Fernández-Tornero, 2023. "Structural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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