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Structural basis of RNA polymerase I pre-initiation complex formation and promoter melting
Pilsl, Michael
and Engel, Christoph
(2020)
Structural basis of RNA polymerase I pre-initiation complex formation and promoter melting.
Nature Communications 11 (1), pp. 1-10.
Date of publication of this fulltext: 09 Apr 2020 16:33
Article
DOI to cite this document: 10.5283/epub.43056
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 ...
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. RNA polymerase I (Pol I) catalyses the transcription of ribosomal RNA precursors, and its transcription initiation mechanism differs from that of Pol II and Pol III. Here the authors present the cryo-EM structure of a trapped early intermediate stage of promoter-recruited Pol I, which reveals the interactions of the basal rDNA transcription machinery with the native promoter, and discuss the mechanistic implications.
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Details
| Item type | Article | ||||
| Journal or Publication Title | Nature Communications | ||||
| Publisher: | Nature | ||||
|---|---|---|---|---|---|
| Open Access Type: | Gold (with APC) | ||||
| Place of Publication: | LONDON | ||||
| Volume: | 11 | ||||
| Number of Issue or Book Chapter: | 1 | ||||
| Page Range: | pp. 1-10 | ||||
| Date | 5 March 2020 | ||||
| Institutions | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie | ||||
| Projects |
Funded by:
Deutsche Forschungsgemeinschaft (DFG)
(394580547)
| ||||
| Identification Number |
| ||||
| Keywords | UPSTREAM ACTIVATION FACTOR; TATA-BINDING PROTEIN; TRANSCRIPTION INITIATION; RIBOSOMAL DNA; MOLECULAR-STRUCTURES; ELONGATION COMPLEX; CRYSTAL-STRUCTURE; TIF-IA; YEAST; TFIIB; | ||||
| Dewey Decimal Classification | 500 Science > 570 Life sciences | ||||
| Status | Published | ||||
| Refereed | Yes, this version has been refereed | ||||
| Created at the University of Regensburg | Yes | ||||
| URN of the UB Regensburg | urn:nbn:de:bvb:355-epub-430569 | ||||
| Item ID | 43056 |
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