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9T5H

RNA polymerase II bound to Gdown1 and RPAP2

Summary for 9T5H
Entry DOI10.2210/pdb9t5h/pdb
EMDB information55579 55580 55581 55582 55583
DescriptorDNA-directed RNA polymerase subunit, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11-a, ... (15 entities in total)
Functional Keywordscytoplasm, polymerase, biogenesis, transcription
Biological sourceHomo sapiens (human)
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Total number of polymer chains14
Total formula weight629278.54
Authors
Hlavata, A.,Bernecky, C. (deposition date: 2025-11-05, release date: 2026-07-15, Last modification date: 2026-07-22)
Primary citationHlavata, A.,Neuditschko, B.,Schellhaas, U.,Plaschka, C.,Herzog, F.,Bernecky, C.
Structure of cytoplasmic RNA polymerase II.
Nat Commun, 2026
Cited by
PubMed Abstract: RNA polymerase II (Pol II) must be assembled in the cytoplasm before it enters the nucleus, where it transcribes protein-coding genes. Although transcription by Pol II is intensively studied, how this central multi-subunit enzyme is made and the role of dedicated assembly factors remains unclear. Here, we report the integrative structural analysis of a native human Pol II from the cytoplasm captured near the end of biogenesis. The complex contains Gdown1 and three biogenesis factors - RPAP2 and the critical small GTPases GPN1 and GPN3. Cryo-EM analysis of the complex reveals how Gdown1 and RPAP2 associate with Pol II and prevent the premature association of transcription factors. Further biochemical and cryo-EM analysis reveals how RPAP2 tethers GPN1-GPN3 to the complex and how the assembly of the RPAP2-GPN1-GPN3 complex is controlled by GTP hydrolysis. The combined results uncover a network of interactions that chaperone cytoplasmic Pol II to prevent aberrant interactions, reveal a molecular switch regulating biogenesis factor association, and suggest a general mechanism for the action of GPN-loop GTPase family of enzymes.
PubMed: 42443208
DOI: 10.1038/s41467-026-75416-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.7 Å)
Structure validation

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