Published In
Nature Communications
Document Type
Article
Publication Date
11-2020
Subjects
RNA -- analysis, Gene expression, RNA, Ribosomes
Abstract
Opening of the DNA binding cleft of cellular RNA polymerase (RNAP) is necessary for transcription initiation but the underlying molecular mechanism is not known. Here, we report on the cryo-electron microscopy structures of the RNAP, RNAP-TFEα binary, and RNAPTFEα-promoter DNA ternary complexes from archaea, Thermococcus kodakarensis (Tko). The structures reveal that TFEα bridges the RNAP clamp and stalk domains to open the DNA binding cleft. Positioning of promoter DNA into the cleft closes it while maintaining the TFEα interactions with the RNAP mobile modules. The structures and photo-crosslinking results also suggest that the conserved aromatic residue in the extended winged-helix domain of TFEα interacts with promoter DNA to stabilize the transcription bubble. This study provides a structural basis for the functions of TFEα and elucidates the mechanism by which the DNA binding cleft is opened during transcription initiation in the stalk-containing RNAPs, including archaeal and eukaryotic RNAPs.
Rights
This work is licensed under a Creative Commons Attribution 4.0 International License.
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DOI
10.1038/s41467-020-19998-x
Persistent Identifier
https://archives.pdx.edu/ds/psu/34377
Citation Details
Jun, S. H., Hyun, J., Cha, J. S., Kim, H., Bartlett, M. S., Cho, H. S., & Murakami, K. S. (2020). Direct binding of TFEα opens DNA binding cleft of RNA polymerase. Nature Communications, 11(1), 1-12.
