Tetrameric architecture of an active phenol-bound form of the AAA
| Autor: | Kwang-Hyun, Park, Sungchul, Kim, Su-Jin, Lee, Jee-Eun, Cho, Vinod Vikas, Patil, Arti Baban, Dumbrepatil, Hyung-Nam, Song, Woo-Chan, Ahn, Chirlmin, Joo, Seung-Goo, Lee, Victoria, Shingler, Eui-Jeon, Woo |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Adenosine Triphosphatases
Binding Sites Phenol Sequence Homology Amino Acid Protein Conformation Pseudomonas putida DNA-Directed RNA Polymerases Gene Expression Regulation Bacterial Article DNA-Binding Proteins Adenosine Triphosphate Bacterial Proteins Single-molecule biophysics Trans-Activators Amino Acid Sequence Protein Multimerization Protein Binding X-ray crystallography |
| Zdroj: | Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | 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. DmpR is a bacterial enhancer binding protein from the AAA+ family of ATPases that binds aromatic compounds and controls the transcription of genes involved in the degradation of toxic pollutants. Here, the authors present the crystal structure of phenol-bound DmpR, which forms a tetramer and discuss its signal transduction mechanism. |
| Databáze: | OpenAIRE |
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