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Journal Article

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

MPS-Authors
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Xu,  Y.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Bernecky,  C.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons188023

Lee,  C. T.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

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Maier,  K. C.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons173057

Schwalb,  B.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Tegunov,  D.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

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Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Fulltext (public)

2451197.pdf
(Publisher version), 3MB

Supplementary Material (public)

2451197_Suppl_1.pdf
(Supplementary material), 2MB

2451197_Suppl_2.xlsx
(Supplementary material), 40KB

Citation

Xu, Y., Bernecky, C., Lee, C. T., Maier, K. C., Schwalb, B., Tegunov, D., et al. (2017). Architecture of the RNA polymerase II-Paf1C-TFIIS transcription elongation complex. Nature Communications, 8: 15741. doi:10.1038/ncomms15741.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-5BA8-1
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.