ArticleNucleic acids research2019
Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in Deinococcus.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Rising from the fragments: a multi-factorial regulatory framework of DNA damage response in Deinococcus radiodurans.Extremophiles : life under extreme conditions · 2026Review
- Molecular mechanism of a single stranded DNA-stimulated bacterial immune peptidase.bioRxiv : the preprint server for biology · 2026Article
- Radiation-response inFEMS microbes · 2026Article
- NsrM (All0345) and NsrX (Alr1976), two FurC (PerR)-targeted transcriptional regulators, modulate nitrogen metabolism and heterocyst differentiation genes in the cyanobacteriumMicrobiology spectrum · 2025Article
- Chromosomal Curing Drives an Arms Race Between Bacterial Transformation and Prophage.Molecular biology and evolution · 2025Article
- Bacterial PprI-DdrO system evolved from ImmA-ImmR system in the prophage.Protein science : a publication of the Protein Society · 2025Article
- DdiA, an XRE family transcriptional regulator, is a co-regulator of the DNA damage response inJournal of bacteriology · 2025Article
- Article
- The Deinococcus protease PprI senses DNA damage by directly interacting with single-stranded DNA.Nature communications · 2024Article
- A conserved signaling pathway activates bacterial CBASS immune signaling in response to DNA damage.The EMBO journal · 2022Article
- Structural and functional characterization of DdrC, a novel DNA damage-induced nucleoid associated protein involved in DNA compaction.Nucleic acids research · 2022Article
- Characterization of the Radiation Desiccation Response Regulon of the Radioresistant BacteriumCells · 2021Article
- Coexistence of SOS-Dependent and SOS-Independent Regulation of DNA Repair Genes in Radiation-ResistantCells · 2021Review
- Redox signaling through zinc activates the radiation response in Deinococcus bacteria.Scientific reports · 2021Article
- Characteristic and role of chromosomal type II toxin-antitoxin systems locus in Enterococcus faecalis ATCC29212.Journal of microbiology (Seoul, Korea) · 2020Article
- PprI: The Key Protein in Response to DNA Damage inFrontiers in cell and developmental biology · 2020Review
- Structural features and functional implications of proteins enabling the robustness ofComputational and structural biotechnology journal · 2020Review
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
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 repressor 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 dimerization. Cleavage by IrrE occurs in the loop between the last two helices of DdrO and abolishes dimerization 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 oligomerization without cleavage of the XRE repressor.
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