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Molecular mechanism of promoter opening by RNA polymerase III

Author

Listed:
  • Matthias K. Vorländer

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit)

  • Heena Khatter

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit)

  • Rene Wetzel

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit)

  • Wim J. H. Hagen

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit)

  • Christoph W. Müller

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit)

Abstract

RNA polymerase III (Pol III) and transcription factor IIIB (TFIIIB) assemble together on different promoter types to initiate the transcription of small, structured RNAs. Here we present structures of Pol III preinitiation complexes, comprising the 17-subunit Pol III and the heterotrimeric transcription factor TFIIIB, bound to a natural promoter in different functional states. Electron cryo-microscopy reconstructions, varying from 3.7 Å to 5.5 Å resolution, include two early intermediates in which the DNA duplex is closed, an open DNA complex, and an initially transcribing complex with RNA in the active site. Our structures reveal an extremely tight, multivalent interaction between TFIIIB and promoter DNA, and explain how TFIIIB recruits Pol III. Together, TFIIIB and Pol III subunit C37 activate the intrinsic transcription factor-like activity of the Pol III-specific heterotrimer to initiate the melting of double-stranded DNA, in a mechanism similar to that of the Pol II system.

Suggested Citation

  • Matthias K. Vorländer & Heena Khatter & Rene Wetzel & Wim J. H. Hagen & Christoph W. Müller, 2018. "Molecular mechanism of promoter opening by RNA polymerase III," Nature, Nature, vol. 553(7688), pages 295-300, January.
    • Handle: RePEc:nat:nature:v:553:y:2018:i:7688:d:10.1038_nature25440
    DOI: 10.1038/nature25440
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    Cited by:

    1. Haifeng Hou & Yan Li & Mo Wang & Aijun Liu & Zishuo Yu & Ke Chen & Dan Zhao & Yanhui Xu, 2021. "Structural insights into RNA polymerase III-mediated transcription termination through trapping poly-deoxythymidine," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    2. Saurabh Mishra & Shaina H. Hasan & Rima M. Sakhawala & Shereen Chaudhry & Richard J. Maraia, 2021. "Mechanism of RNA polymerase III termination-associated reinitiation-recycling conferred by the essential function of the N terminal-and-linker domain of the C11 subunit," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    3. 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.
    4. Guillermo Abascal-Palacios & Laura Jochem & Carlos Pla-Prats & Fabienne Beuron & Alessandro Vannini, 2021. "Structural basis of Ty3 retrotransposon integration at RNA Polymerase III-transcribed genes," Nature Communications, Nature, vol. 12(1), pages 1-11, December.

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