%0 Journal Article %T Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in Deinococcus %+ Microbiologie Environnementale et Moléculaire (MEM) %+ Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) (BIAM) %+ Institut de Biologie Intégrative de la Cellule (I2BC) %+ Radiorésistance des bactéries et des archées (RBA) %+ Régulateurs du développement de la fleur (Flo_RE) %+ Interactions Protéine Métal (IPM) %+ Institut Paoli-Calmettes (IPC) %A de Groot, Arjan %A Siponen, Marina, I. %A Magerand, Romaric %A Eugenie, Nicolas %A Martin-Arevalillo, Raquel %A Doloy, Jade %A Lemaire, David %A Brandelet, Géraldine %A Parcy, François %A Dumas, Renaud %A Roche, Philippe %A Servant, Pascale %A Confalonieri, Fabrice %A Arnoux, Pascal %A Pignol, David %A Blanchard, Laurence %< avec comité de lecture %@ 0305-1048 %J Nucleic Acids Research %I Oxford University Press %V 47 %N 21 %P 11403–11417 %8 2019 %D 2019 %R 10.1093/nar/gkz883 %M 31598697 %Z Life Sciences [q-bio] %Z Life Sciences [q-bio]/Biochemistry, Molecular Biology %Z Life Sciences [q-bio]/Human health and pathologyJournal articles %X Exposure to harmful conditions such as radiation and desiccation induce oxidative stress and DNA damage. In radiation-resistant Deinococcus bacteria, the radiation/desiccation response is controlled by two proteins: the XRE family transcriptional repres-sor DdrO and the COG2856 metalloprotease IrrE. The latter cleaves and inactivates DdrO. Here, we report the biochemical characterization and crystal structure of DdrO, which is the first structure of a XRE protein targeted by a COG2856 protein. DdrO is composed of two domains that fold independently and are separated by a flexible linker. The N-terminal domain corresponds to the DNA-binding domain. The C-terminal domain, containing three alpha helices arranged in a novel fold, is required for DdrO dimeriza-tion. Cleavage by IrrE occurs in the loop between the last two helices of DdrO and abolishes dimeriza-tion and DNA binding. The cleavage site is hidden in the DdrO dimer structure, indicating that IrrE cleaves DdrO monomers or that the interaction with IrrE induces a structural change rendering accessible the cleavage site. Predicted COG2856/XRE regulatory protein pairs are found in many bacteria, and available data suggest two different molecular mechanisms for stress-induced gene expression: COG2856 protein-mediated cleavage or inhibition of oligomer-ization without cleavage of the XRE repressor. %G English %2 https://cea.hal.science/cea-02315882/document %2 https://cea.hal.science/cea-02315882/file/DeGroot-2019-NAR-gkz883.pdf %L cea-02315882 %U https://cea.hal.science/cea-02315882 %~ INSERM %~ CEA %~ UGA %~ CNRS %~ UNIV-AMU %~ INRA %~ IRTSV-PCV %~ DSV %~ CEA-UPSAY %~ I2BC %~ UNIV-PARIS-SACLAY %~ AGREENIUM %~ CEA-UPSAY-SACLAY %~ JOLIOT %~ CEA-DRF %~ BIG %~ CEA-CAD %~ BIAM %~ IRIG %~ CEA-GRE %~ INRAE %~ TEST-HALCNRS %~ UGA-COMUE %~ ANR %~ GS-ENGINEERING %~ GS-BIOSPHERA %~ GS-HEALTH-DRUG-SCIENCES %~ INSTITUT-SCIENCES-LUMIERE