한빛사 논문
Kwang-Hyun Park1,6, Sungchul Kim2,6, Su-Jin Lee1,3, Jee-Eun Cho1, Vinod Vikas Patil1,3, Arti Baban Dumbrepatil1, Hyung-Nam Song1, Woo-Chan Ahn1, Chirlmin Joo2,*, Seung-Goo Lee4, Victoria Shingler5 & Eui-Jeon Woo1,3,*
1Disease Target Structure Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 305-806, Republic of Korea.
2Kavli Institute of Nanoscience and Department of Bionanoscience, Delft University of Technology, 2629 HZ Delft, The Netherlands.
3Department of Proteome Structural Biology, KRIBB School of Bioscience, University of Science and Technology (UST), Daejeon 305-333, Republic of Korea.
4Synthetic Biology and Bioengineering Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 305-806, Republic of Korea.
5Department of Molecular Biology, Umeå University, 90187 Umeå, SE, Sweden.
6These authors contributed equally: Kwang-Hyun Park, Sungchul Kim.
*Corresponding author
Abstract
The Pseudomonas putida phenol-responsive regulator DmpR is a bacterial enhancer binding protein (bEBP) from the AAA+ ATPase family. Even though it was discovered more than two decades ago and has been widely used for aromatic hydrocarbon sensing, the activation mechanism of DmpR has remained elusive. Here, we show that phenol-bound DmpR forms a tetramer composed of two head-to-head dimers in a head-to-tail arrangement. The DmpR-phenol complex exhibits altered conformations within the C-termini of the sensory domains and shows an asymmetric orientation and angle in its coiled-coil linkers. The structural changes within the phenol binding sites and the downstream ATPase domains suggest that the effector binding signal is propagated through the coiled-coil helixes. The tetrameric DmpR-phenol complex interacts with the σ54 subunit of RNA polymerase in presence of an ATP analogue, indicating that DmpR-like bEBPs tetramers utilize a mechanistic mode distinct from that of hexameric AAA+ ATPases to activate σ54-dependent transcription.
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TOP52020년 후보
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