Journal
NUCLEIC ACIDS RESEARCH
Volume 49, Issue 18, Pages 10747-10755Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkab783
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Funding
- H2020 Marie Curie Individual Fellowship [894862]
- Deutsche Forschungsgemeinschaft [EXC 2067/1 39072994, SFB860, SPP2191]
- ERC Advanced Investigator Grant CHROMATRANS [882357]
- Max Planck Society
- Marie Curie Actions (MSCA) [894862] Funding Source: Marie Curie Actions (MSCA)
- European Research Council (ERC) [882357] Funding Source: European Research Council (ERC)
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The study presents the structure of a mammalian Pol II dimer, showing its distinct features from the Pol I dimer and suggesting that the Pol II dimer may represent an inactive storage form of the polymerase.
Eukaryotic gene transcription is carried out by three RNA polymerases: Pol I, Pol II and Pol III. Although it has long been known that Pol I can form homodimers, it is unclear whether and how the two other RNA polymerases dimerize. Here we present the cryoelectron microscopy (cryo-EM) structure of a mammalian Pol II dimer at 3.5 angstrom resolution. The structure differs from the Pol I dimer and reveals that one Pol II copy uses its RPB4-RPB7 stalk to penetrate the active centre cleft of the other copy, and vice versa, giving rise to a molecular handshake. The polymerase clamp domain is displaced and mobile, and the RPB7 oligonucleotide-binding fold mimics the DNA-RNA hybrid that occupies the cleft during active transcription. The Pol II dimer is incompatible with nucleic acid binding as required for transcription and may represent an inactive storage form of the polymerase.
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