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-Structure paper
タイトル | Direct binding of TFEα opens DNA binding cleft of RNA polymerase. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 6123, Year 2020 |
掲載日 | 2020年11月30日 |
![]() | Sung-Hoon Jun / Jaekyung Hyun / Jeong Seok Cha / Hoyoung Kim / Michael S Bartlett / Hyun-Soo Cho / Katsuhiko S Murakami / ![]() ![]() ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 2.6 - 3.97 Å |
構造データ | ![]() PDB-6kf3: ![]() PDB-6kf4: ![]() PDB-6kf9: ![]() PDB-6pln: ![]() PDB-6xjf: |
化合物 | ![]() ChemComp-MG: ![]() ChemComp-ZN: ![]() ChemComp-HOH: |
由来 |
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![]() | TRANSCRIPTION / apo-RNA polymerase / TFE / general transcription factor |