7MKA
Structure of EC+EC (leading EC-focused)
Summary for 7MKA
Entry DOI | 10.2210/pdb7mka/pdb |
Related | 7MEI |
EMDB information | 23888 |
Descriptor | DNA (40-MER), DNA-directed RNA polymerases I, II, and III subunit RPABC3, DNA-directed RNA polymerase II subunit RPB9, ... (17 entities in total) |
Functional Keywords | pol ii, transcription |
Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
Total number of polymer chains | 15 |
Total formula weight | 544039.81 |
Authors | Yang, C.,Murakami, K. (deposition date: 2021-04-22, release date: 2022-04-27, Last modification date: 2024-10-30) |
Primary citation | Yang, C.,Fujiwara, R.,Kim, H.J.,Basnet, P.,Zhu, Y.,Gorbea Colon, J.J.,Steimle, S.,Garcia, B.A.,Kaplan, C.D.,Murakami, K. Structural visualization of de novo transcription initiation by Saccharomyces cerevisiae RNA polymerase II. Mol.Cell, 82:660-676.e9, 2022 Cited by PubMed Abstract: Previous structural studies of the initiation-elongation transition of RNA polymerase II (pol II) transcription have relied on the use of synthetic oligonucleotides, often artificially discontinuous to capture pol II in the initiating state. Here, we report multiple structures of initiation complexes converted de novo from a 33-subunit yeast pre-initiation complex (PIC) through catalytic activities and subsequently stalled at different template positions. We determine that PICs in the initially transcribing complex (ITC) can synthesize a transcript of ∼26 nucleotides before transitioning to an elongation complex (EC) as determined by the loss of general transcription factors (GTFs). Unexpectedly, transition to an EC was greatly accelerated when an ITC encountered a downstream EC stalled at promoter proximal regions and resulted in a collided head-to-end dimeric EC complex. Our structural analysis reveals a dynamic state of TFIIH, the largest of GTFs, in PIC/ITC with distinct functional consequences at multiple steps on the pathway to elongation. PubMed: 35051353DOI: 10.1016/j.molcel.2021.12.020 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.54 Å) |
Structure validation
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