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The cryo-EM structure of a 12-subunit variant of RNA polymerase I reveals dissociation of the A49-A34. 5 heterodimer and rearrangement of subunit A12. 2

Elife. 2019-03; 
Tafur L,, Sadian Y, Hanske J, Wetzel R, Weis F, Müller CW.
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摘要

RNA polymerase (Pol) I is a 14-subunit enzyme that solely transcribes pre-ribosomal RNA. Cryo-electron microscopy (EM) structures of Pol I initiation and elongation complexes have given first insights into the molecular mechanisms of Pol I transcription. Here, we present cryo-EM structures of yeast Pol I elongation complexes (ECs) bound to the nucleotide analog GMPCPP at 3.2 to 3.4 Å resolution that provide additional insight into the functional interplay between the Pol I-specific transcription-like factors A49-A34.5 and A12.2. Strikingly, most of the nucleotide-bound ECs lack the A49-A34.5 heterodimer and adopt a Pol II-like conformation, in which the A12.2 C-terminal domain is bound in a previously unobserv... More

关键词

RNA polymerase I; S. cerevisiae; chromosomes; elongation complex; gene expression; molecular biophysics; ribosomal RNA synthesis; structural biology; transcription regulation