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The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans

URN to cite this document:
urn:nbn:de:bvb:355-epub-528607
DOI to cite this document:
10.5283/epub.52860
Daiß, Julia L. ; Pilsl, Michael ; Straub, Kristina ; Bleckmann, Andrea ; Höcherl, Mona ; Heiss, Florian B. ; Abascal-Palacios, Guillermo ; Ramsay, Ewan Phillip ; Tlučková, Katarina ; Mars, Jean-Clement ; Fürtges, Torben ; Bruckmann, Astrid ; Rudack, Till ; Bernecky, Carrie ; Lamour, Valérie ; Panov, Konstantin ; Vannini, Alessandro ; Moss, Tom ; Engel, Christoph
[img]License: Creative Commons Attribution 4.0
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Date of publication of this fulltext: 09 Sep 2022 12:41



Abstract

Transcription of the ribosomal RNA precursor by RNA polymerase (Pol) I is a major determinant of cellular growth, and dysregulation is observed in many cancer types. Here, we present the purification of human Pol I from cells carrying a genomic GFP fusion on the largest subunit allowing the structural and functional analysis of the enzyme across species. In contrast to yeast, human Pol I carries ...

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