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Journal Article

Architecture of initiation-competent 12-subunit RNA polymerase II

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Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Armache, K. J., Kettenberger, H., & Cramer, P. (2003). Architecture of initiation-competent 12-subunit RNA polymerase II. Proceedings of the National Academy of Sciences of the USA, 100(12), 6964-6968. doi:10.1073/pnas.1030608100.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-86A7-1
Abstract
RNA polymerase (Pol) II consists of a 10-polypeptide catalytic core and the two-subunit Rpb47 complex that is required for transcription initiation. Previous structures of the Pol II core revealed a ‘‘clamp,’’ which binds the DNA template strand via three ‘‘switch regions,’’ and a flexible ‘‘linker’’ to the C-terminal repeat domain (CTD). Here we derived a model of the complete Pol II by fitting structures of the core and Rpb47 to a 4.2-Å crystallographic electron density map. Rpb47 protrudes from the polymerase ‘‘upstream face,’’ on which initiation factors assemble for promoter DNA loading. Rpb7 forms a wedge between the clamp and the linker, restricting the clamp to a closed position. The wedge allosterically prevents entry of the promoter DNA duplex into the active center cleft and induces in two switch regions a conformation poised for template-strand binding. Interaction of Rpb47 with the linker explains Rpb4-mediated recruitment of the CTD phosphatase to the CTD during Pol II recycling. The core–Rpb7 interaction and some functions of Rpb47 are apparently conserved in all eukaryotic and archaeal RNA polymerases but not in the bacterial enzyme.