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Architecture of the RNA polymerase II-Paf1C-TFIIS transcription elongation complex

Author

Listed:
  • Youwei Xu

    (Max-Planck-Institute for Biophysical Chemistry, Max Planck Society)

  • Carrie Bernecky

    (Max-Planck-Institute for Biophysical Chemistry, Max Planck Society)

  • Chung-Tien Lee

    (Bioanalytical Mass Spectrometry, Max-Planck-Institute for Biophysical Chemistry
    Bioanalytics Group, Institute for Clinical Chemistry, University Medical Center, Göttingen)

  • Kerstin C. Maier

    (Max-Planck-Institute for Biophysical Chemistry, Max Planck Society)

  • Björn Schwalb

    (Max-Planck-Institute for Biophysical Chemistry, Max Planck Society)

  • Dimitry Tegunov

    (Max-Planck-Institute for Biophysical Chemistry, Max Planck Society)

  • Jürgen M. Plitzko

    (Max-Planck-Institute for Biochemistry)

  • Henning Urlaub

    (Bioanalytical Mass Spectrometry, Max-Planck-Institute for Biophysical Chemistry
    Bioanalytics Group, Institute for Clinical Chemistry, University Medical Center, Göttingen)

  • Patrick Cramer

    (Max-Planck-Institute for Biophysical Chemistry, Max Planck Society)

Abstract

The conserved polymerase-associated factor 1 complex (Paf1C) plays multiple roles in chromatin transcription and genomic regulation. Paf1C comprises the five subunits Paf1, Leo1, Ctr9, Cdc73 and Rtf1, and binds to the RNA polymerase II (Pol II) transcription elongation complex (EC). Here we report the reconstitution of Paf1C from Saccharomyces cerevisiae, and a structural analysis of Paf1C bound to a Pol II EC containing the elongation factor TFIIS. Cryo-electron microscopy and crosslinking data reveal that Paf1C is highly mobile and extends over the outer Pol II surface from the Rpb2 to the Rpb3 subunit. The Paf1-Leo1 heterodimer and Cdc73 form opposite ends of Paf1C, whereas Ctr9 bridges between them. Consistent with the structural observations, the initiation factor TFIIF impairs Paf1C binding to Pol II, whereas the elongation factor TFIIS enhances it. We further show that Paf1C is globally required for normal mRNA transcription in yeast. These results provide a three-dimensional framework for further analysis of Paf1C function in transcription through chromatin.

Suggested Citation

  • Youwei Xu & Carrie Bernecky & Chung-Tien Lee & Kerstin C. Maier & Björn Schwalb & Dimitry Tegunov & Jürgen M. Plitzko & Henning Urlaub & Patrick Cramer, 2017. "Architecture of the RNA polymerase II-Paf1C-TFIIS transcription elongation complex," Nature Communications, Nature, vol. 8(1), pages 1-13, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15741
    DOI: 10.1038/ncomms15741
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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.

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