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Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in Deinococcus

Arjan de Groot 1 Marina Siponen 2, 1 Romaric Magerand 1 Nicolas Eugenie 3, 4 Raquel Martin-Arevalillo 5 Jade Doloy 1 David Lemaire 6 Géraldine Brandelet 1 François Parcy 5 Renaud Dumas 5 Philippe Roche 7 Pascale Servant 3, 4 Fabrice Confalonieri 3, 4 Pascal Arnoux 1 David Pignol 1 Laurence Blanchard 1
1 MEM - Microbiologie Environnementale et Moléculaire
BIAM - Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) : DRF/BIAM
2 BIAM - Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB)
3 I2BC - Institut de Biologie Intégrative de la Cellule
4 RBA - Radiorésistance des bactéries et des archées
DBG - Département Biologie des Génomes
5 Flo_RE - Régulateurs du développement de la fleur
LPCV - Physiologie cellulaire et végétale
6 IPM - Interactions Protéine Métal
BIAM - Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) : DRF/BIAM
7 Institut Paoli-Calmettes
Abstract : 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.
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CEA | UNIV-AMU | CEA-GRE | JOLIOT | BIAM | IRIG | CEA-CAD | CEA-DRF | I2BC | CNRS | IRTSV-PCV | INRA | CEA-UPSAY | INRAE | UGA

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Arjan de Groot, Marina Siponen, Romaric Magerand, Nicolas Eugenie, Raquel Martin-Arevalillo, et al.. Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in Deinococcus. Nucleic Acids Research, Oxford University Press, 2019, 47 (21), pp.11403-11417. ⟨10.1093/nar/gkz883⟩. ⟨cea-02315882⟩

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