Structure and DNA damage-dependent derepression mechanism for the XRE family member DG-DdrO
| Autor: | Kaiying Cheng, Yuejin Hua, Huizhi Lu, Hong Xu, Chaoming Pan, Ye Zhao, Yuxia Luo, Li Shengjie, Liangyan Wang, Bing Tian |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
DNA damage
Helix-turn-helix Biology DNA-binding protein Protein Structure Secondary 03 medical and health sciences chemistry.chemical_compound Protein structure Bacterial Proteins Structural Biology Genetics Deinococcus Amino Acid Sequence Promoter Regions Genetic Helix-Turn-Helix Motifs 030304 developmental biology 0303 health sciences 030306 microbiology Promoter Gene Expression Regulation Bacterial biology.organism_classification Cell biology chemistry Metalloproteases Deinococcus geothermalis DNA DNA Damage Protein Binding Transcription Factors |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| Popis: | DdrO is an XRE family transcription repressor that, in coordination with the metalloprotease PprI, is critical in the DNA damage response of Deinococcus species. Here, we report the crystal structure of Deinococcus geothermalis DdrO. Biochemical and structural studies revealed the conserved recognizing α-helix and extended dimeric interaction of the DdrO protein, which are essential for promoter DNA binding. Two conserved oppositely charged residues in the HTH motif of XRE family proteins form salt bridge interactions that are essential for promoter DNA binding. Notably, the C-terminal domain is stabilized by hydrophobic interactions of leucine/isoleucine-rich helices, which is critical for DdrO dimerization. Our findings suggest that DdrO is a novel XRE family transcriptional regulator that forms a distinctive dimer. The structure also provides insight into the mechanism of DdrO-PprI-mediated DNA damage response in Deinococcus. |
| Databáze: | OpenAIRE |
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