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Structural rearrangement of TFIIS- and TFIIE/TFIIF-like subunits in RNA polymerase I transcription complexes

View ORCID ProfileLucas Tafur, Yashar Sadian, Rene Wetzel, Felix Weis, View ORCID ProfileChristoph W. Müller
doi: https://doi.org/10.1101/353136
Lucas Tafur
1European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
2Joint PhD degree from EMBL and Heidelberg University, Faculty of Biosciences
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Yashar Sadian
1European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
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Rene Wetzel
1European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
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Felix Weis
1European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
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Christoph W. Müller
1European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
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  • ORCID record for Christoph W. Müller
  • For correspondence: cmueller@embl.de
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Abstract

RNA polymerase (Pol) I is a 14-subunit enzyme that solely transcribes pre-ribosomal RNA. Cryo-EM structures of Pol I initiation and elongation complexes have given first insights into the molecular mechanisms of Pol I transcription. Here, we present cryo-electron microscopy structures of yeast Pol I elongation complexes (ECs) bound to the nucleotide analog GMPCPP at 3.2 to 3.4 Å resolution that provide additional insight into the functional interplay between the TFIIE/TFIIF-like A49-A34.5 heterodimer and the TFIIS-like subunit A12.2 present in Pol I. Strikingly, most of the nucleotide-bound ECs lack the A49-A34.5 heterodimer and adopt a Pol II-like conformation, in which the A12.2 C-terminal domain is bound in a previously unobserved position at the A135 surface. Our work suggests a regulatory mechanism of Pol I transcription where the association of the A49-A34.5 heterodimer to Pol I is regulated by subunit A12.2, thereby explaining in vitro biochemical and kinetic data.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted July 03, 2018.
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Structural rearrangement of TFIIS- and TFIIE/TFIIF-like subunits in RNA polymerase I transcription complexes
Lucas Tafur, Yashar Sadian, Rene Wetzel, Felix Weis, Christoph W. Müller
bioRxiv 353136; doi: https://doi.org/10.1101/353136
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Structural rearrangement of TFIIS- and TFIIE/TFIIF-like subunits in RNA polymerase I transcription complexes
Lucas Tafur, Yashar Sadian, Rene Wetzel, Felix Weis, Christoph W. Müller
bioRxiv 353136; doi: https://doi.org/10.1101/353136

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