6TPS
early intermediate RNA Polymerase I Pre-initiation complex - eiPIC
Summary for 6TPS
Entry DOI | 10.2210/pdb6tps/pdb |
EMDB information | 10544 |
Descriptor | DNA-directed RNA polymerase I subunit RPA190, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerases I and III subunit RPAC2, ... (24 entities in total) |
Functional Keywords | transcription initiation, ribosome biosynthesis, rna polymerase i, transcription |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) More |
Total number of polymer chains | 22 |
Total formula weight | 880407.53 |
Authors | |
Primary citation | Pilsl, M.,Engel, C. Structural basis of RNA polymerase I pre-initiation complex formation and promoter melting. Nat Commun, 11:1206-1206, 2020 Cited by PubMed Abstract: Transcription of the ribosomal RNA precursor by RNA polymerase (Pol) I is a prerequisite for the biosynthesis of ribosomes in eukaryotes. Compared to Pols II and III, the mechanisms underlying promoter recognition, initiation complex formation and DNA melting by Pol I substantially diverge. Here, we report the high-resolution cryo-EM reconstruction of a Pol I early initiation intermediate assembled on a double-stranded promoter scaffold that prevents the establishment of downstream DNA contacts. Our analyses demonstrate how efficient promoter-backbone interaction is achieved by combined re-arrangements of flexible regions in the 'core factor' subunits Rrn7 and Rrn11. Furthermore, structure-function analysis illustrates how destabilization of the melted DNA region correlates with contraction of the polymerase cleft upon transcription activation, thereby combining promoter recruitment with DNA-melting. This suggests that molecular mechanisms and structural features of Pol I initiation have co-evolved to support the efficient melting, initial transcription and promoter clearance required for high-level rRNA synthesis. PubMed: 32139698DOI: 10.1038/s41467-020-15052-y PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.54 Å) |
Structure validation
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