Zu Hauptinhalt springen

Research

Research Topic

Assembly of eukaryotic ribosomes requires four ribosomal RNAs (rRNAs). The nascent ribosomal RNA precursor contains three of these rRNAs and is transcribed by the RNA polymerase (Pol) I machinery.

Using a structural biology hybrid approach and in vitro biochemistry structure-function analyses we study the molecular basis of Pol I transcription and its regulation. In combination with ex vivo and in-cell techniques, we correlate our findings with the in vivo situation.


The RNA polymerase I transcription initiation system

(DFG-funded 'Emmy Noether' project)

Cramer Engel Whole Op Pol I

Cryo-EM reconstruction of the yeast RNA polymerase I early initiation intermediate including Rrn3 and Core Factor (Pilsl & Engel, Nature Communications 2020)

Combining X-ray crystallography with recent advances in cryo-electron microscopy (cryo-EM) now allows the application of an integrated structural biology hybrid approach for the analysis of transiently stable, multi-protein DNA/RNA complexes. Continuing and expanding the structural analysis of Pol I and its transcription machinery with this integrated approach allowed us to get insight into the structural basis of transcription initiation (Engel et al., Nature Communications 2016; and Engel et al., Cell 2017). We further analyzes the mechanisms of promoter recognition and DNA-duplex melting (Pilsl and Engel, Nature Communications 2020). Now, we are now interested in understanding the structural and functional basis of Pol I promoter targeting and escape in a close-to-native environment.


Mechanisms of transcription by RNA polymerase I

(SFB 960 project A8)

Cryo-EM reconstruction of the S. pombe RNA polymerase I actively elongting complex and inactive Pol I dimer (Heiss, Dai?, Becker and Engel, Nature Communications 2020)

Structural analysis of Pol I and its transcription machinery has revealed striking differences but also many similarities with Pol II and Pol III. This was demonstrated by the 3D structure of the entire 14-subunit, 590 kDa Pol I enzyme from yeast solved by X-ray crystallography (Engel et al., Nature 2013). We are now interested in studying structure-function relationships in Pol I transcription throughout organisms to understand the molecul