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Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2
Structural highlights
FunctionI3LJR4_PIG DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279] Publication Abstract from PubMedNuclear import of RNA polymerase II (Pol II) involves the conserved factor RPAP2. Here we report the cryo-electron microscopy (cryo-EM) structure of mammalian Pol II in complex with human RPAP2 at 2.8 A resolution. The structure shows that RPAP2 binds between the jaw domains of the polymerase subunits RPB1 and RPB5. RPAP2 is incompatible with binding of downstream DNA during transcription and is displaced upon formation of a transcription pre-initiation complex. Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2.,Fianu I, Dienemann C, Aibara S, Schilbach S, Cramer P Commun Biol. 2021 May 21;4(1):606. doi: 10.1038/s42003-021-02088-z. PMID:34021257[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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