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Pilsl, Michael ; Engel, Christoph

Structural basis of RNA polymerase I pre-initiation complex formation and promoter melting

Pilsl, Michael und Engel, Christoph (2020) Structural basis of RNA polymerase I pre-initiation complex formation and promoter melting. Nature Communications 11 (1), S. 1-10.

Veröffentlichungsdatum dieses Volltextes: 09 Apr 2020 16:33
Artikel
DOI zum Zitieren dieses Dokuments: 10.5283/epub.43056


Zusammenfassung

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

DokumentenartArtikel
Titel eines Journals oder einer ZeitschriftNature Communications
Verlag:Nature
Ort der Veröffentlichung:LONDON
Band:11
Nummer des Zeitschriftenheftes oder des Kapitels:1
Seitenbereich:S. 1-10
Datum5 März 2020
InstitutionenBiologie und Vorklinische Medizin > Institut für Biochemie, Genetik und Mikrobiologie
Projekte
Gefördert von: Deutsche Forschungsgemeinschaft (DFG) (394580547)
Identifikationsnummer
WertTyp
10.1038/s41467-020-15052-yDOI
Stichwörter / KeywordsUPSTREAM ACTIVATION FACTOR; TATA-BINDING PROTEIN; TRANSCRIPTION INITIATION; RIBOSOMAL DNA; MOLECULAR-STRUCTURES; ELONGATION COMPLEX; CRYSTAL-STRUCTURE; TIF-IA; YEAST; TFIIB;
Dewey-Dezimal-Klassifikation500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie
StatusVeröffentlicht
BegutachtetJa, diese Version wurde begutachtet
An der Universität Regensburg entstandenJa
URN der UB Regensburgurn:nbn:de:bvb:355-epub-430569
Dokumenten-ID43056

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