[논문]Direct binding of TFEα opens DNA binding cleft of RNA polymerase

Jun, Sung-Hoon; Hyun, Jaekyung; Cha, Jeong Seok; Kim, Hoyoung; Bartlett, Michael S.; Cho, Hyun-Soo; Murakami, Katsuhiko S.

doi:10.1038/s41467-020-19998-x

[해외논문] Direct binding of TFEα opens DNA binding cleft of RNA polymerase 원문보기

Nature communications, v.11 no.1 = v.11, 2020년, pp.6123 -

Jun, Sung-Hoon (Electron Microscopy Research Center, Korea Basic Science Institute, Chungcheongbukdo, 28119 Republic of Korea) , Hyun, Jaekyung (Electron Microscopy Research Center, Korea Basic Science Institute, Chungcheongbukdo, 28119 Republic of Korea) , Cha, Jeong Seok (Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, 03722 Republic of Korea) , Kim, Hoyoung (Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, 03722 Republic of Korea) , Bartlett, Michael S. (Department of Biology, the Portland State University, Portland, OR 97207 USA) , Cho, Hyun-Soo (Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, 03722 Republic of Korea) , Murakami, Katsuhiko S. (Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802 USA)

Abstract ▼ AI-Helper

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 RNAP-TFEα-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.How clamp conformation is regulated in the transcription cycle of stalk-containing archaeal and eukaryotic RNA polymerase (RNAP) systems is still not well understood. Here, the authors combine cryo-EM, X-ray crystallography and photo-crosslinking assays to structurally characterise RNAP, the RNAP-TFEα binary and RNAP-TFEα-promoter DNA ternary complexes from the archaea Thermococcus kodakarensis and enables them to describe the dynamic conformational changes of the general transcription factor TFEα and RNAP during the early stage of transcription cycle.

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