Conserved architecture of the core RNA polymerase II initiation complex

Wolfgang Mühlbacher, Sarah Sainsbury, Matthias Hemann, Merle Hantsche, Simon Neyer, Franz Herzog () and Patrick Cramer ()
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Wolfgang Mühlbacher: Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25
Sarah Sainsbury: Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25
Matthias Hemann: Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25
Merle Hantsche: Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25
Simon Neyer: Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25
Franz Herzog: Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25
Patrick Cramer: Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25

Nature Communications, 2014, vol. 5, issue 1, 1-6

Abstract: Abstract During transcription initiation at promoters of protein-coding genes, RNA polymerase (Pol) II assembles with TBP, TFIIB and TFIIF into a conserved core initiation complex that recruits additional factors. The core complex stabilizes open DNA and initiates RNA synthesis, and it is conserved in the Pol I and Pol III transcription systems. Here, we derive the domain architecture of the yeast core pol II initiation complex during transcription initiation. The yeast complex resembles the human initiation complex and reveals that the TFIIF Tfg2 winged helix domain swings over promoter DNA. An ‘arm’ and a ‘charged helix’ in TFIIF function in transcription start site selection and initial RNA synthesis, respectively, and apparently extend into the active centre cleft. Our model provides the basis for further structure–function analysis of the entire transcription initiation complex.

Date: 2014
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DOI: 10.1038/ncomms5310

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