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Structural and functional characterization of DdrC, a novel DNA damage-induced nucleoid associated protein involved in DNA compaction
Open accessPreprint — published as 10.1093/nar/gkac563
Abstract
Deinococcus radiodurans is a spherical bacterium well-known for its outstanding resistance to DNA-damaging agents. Exposure to such agents leads to drastic changes in the transcriptome of D. radiodurans . In particular, four Deinococcus -specific genes, known as DNA Damage Response genes, are strongly up-regulated and have been shown to contribute to the resistance phenotype of D. radiodurans . One of these, DdrC, is expressed shortly after exposure to γ-radiation and is rapidly recruited to the nucleoid. In vitro , DdrC has been shown to compact circular DNA, circularize linear DNA, anneal complementary DNA strands and protect DNA from nucleases. To shed light on the possible functions of DdrC in D. radiodurans , we determined the crystal structure of the domain-swapped DdrC dimer at a resolution of 2.2 Å and further characterized its DNA binding and compaction properties. Notably, we show that DdrC bears two asymmetric DNA binding sites located on either side of the dimer and can modulate the topology and level of compaction of circular DNA. These findings suggest that DdrC may be a DNA damage-induced nucleoid-associated protein that enhances nucleoid compaction to limit the dispersion of the fragmented genome and facilitate DNA repair after exposure to severe DNA damaging conditions.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Banneville, A.-S., de la Tour, C. B., Hognon, C., Colletier, J.-P., Teulon, J.-M., Le Roy, A., Pellequer, J.-L., Monari, A., Dehez, F., Confalonieri, F., Servant, P., & Timmins, J.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Timmins, Joanna
- ORCID
- Venue
- Nucleic Acids Research
- Publisher
- openRxiv
- Published
- 2021-10-27
- Volume
- 50
- Issue
- 13
- Pages
- 7680-7696
- ISSN
- 0305-1048 (ISSN-L)
- PMC
- PMC9303277
- OpenAlex
- W4284958032
- Cited by
- 22
- References
- 1
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 8 · 2023: 8 · 2022: 3
- FWCI
- 3.17
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc
- Locations
- Nucleic Acids Research (publishedVersion, cc-by-nc)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by-nc-nd)
- Funders
- Laboratoire d'Excellence SEAM (ANR-11-IDEX-05-02, ANR-11-LABX-086)
- Agence Nationale de la Recherche (ANR-17-EURE-0003, 11 IDEX 05 02, 11 LABX 086, ANR-17-EURE-, ANR-11-IDEX-0502, ANR 11 LABX 086, ANR 11, ANR-10-LABX-0096, ANR-17, ANR-10, ANR11-LABX, ANR-11-IDEX-0005, ANR-10-INBS-0005, ANR-10-LABX-0049)
- European Synchrotron Radiation Facility (ID23‐1)
- Centre National de la Recherche Scientifique (ID23-1, ANR‐17‐EURE‐0003)
- Commissariat Général à l'Investissement (ANR-11-LABX-086, ANR 11 IDEX 05 02)
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives
- French Infrastructure for Integrated Structural Biology (ANR-17-EURE-0003, UMS 3518, ANR-10-INBS-0005, ANR-10-INBS-000502, ANR-10-INBS)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- Deinococcus radiodurans, nucleoid-associated proteins, DNA condensation, DNA damage response, radioresistance (biology), crystal structure, DNA binding sites, DNA topology, DNA repair, genome fragmentation
- MeSH terms
- Bacterial Proteins, DNA Damage, DNA Repair, DNA, Circular, Deinococcus
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