Crystal Structure of the IrrE Protein, a Central Regulator of DNA Damage Repair in Deinococcaceae

Vujicic-Zagar, A.; Dulermo, Rémi; Gorrec, M. Le; Vannier, Françoise; Servant, Pascale; Sommer, Suzanne; Groot, Arjan de; Serre, Laurence

doi:10.1016/j.jmb.2008.12.062

Cited by 73 publications

(110 citation statements)

References 51 publications

(43 reference statements)

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“…However, IrrE does not seem to bind to the promoter region of VOL. 75, 2011 D. RADIODURANS OXIDATIVE STRESS RESISTANCE 165 (203) and may regulate the transcription of genes through a more classic transcription factor (642). The expression of irrE in E. coli slightly enhances the expression of RecA (1.5-fold), radiation resistance (1.6-fold), the scavenging of O 2 ⅐ Ϫ and H 2 O 2 , and both the constitutive (2.4-fold) and radiation-induced (4.3-fold) activities of KatG (203).…”

Section: Stress Response Transcriptional Regulatorsmentioning

confidence: 99%

Oxidative Stress Resistance inDeinococcus radiodurans

Slade

Radman

2011

Microbiol Mol Biol Rev

648

639

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SUMMARY Deinococcus radiodurans is a robust bacterium best known for its capacity to repair massive DNA damage efficiently and accurately. It is extremely resistant to many DNA-damaging agents, including ionizing radiation and UV radiation (100 to 295 nm), desiccation, and mitomycin C, which induce oxidative damage not only to DNA but also to all cellular macromolecules via the production of reactive oxygen species. The extreme resilience of D. radiodurans to oxidative stress is imparted synergistically by an efficient protection of proteins against oxidative stress and an efficient DNA repair mechanism, enhanced by functional redundancies in both systems. D. radiodurans assets for the prevention of and recovery from oxidative stress are extensively reviewed here. Radiation- and desiccation-resistant bacteria such as D. radiodurans have substantially lower protein oxidation levels than do sensitive bacteria but have similar yields of DNA double-strand breaks. These findings challenge the concept of DNA as the primary target of radiation toxicity while advancing protein damage, and the protection of proteins against oxidative damage, as a new paradigm of radiation toxicity and survival. The protection of DNA repair and other proteins against oxidative damage is imparted by enzymatic and nonenzymatic antioxidant defense systems dominated by divalent manganese complexes. Given that oxidative stress caused by the accumulation of reactive oxygen species is associated with aging and cancer, a comprehensive outlook on D. radiodurans strategies of combating oxidative stress may open new avenues for antiaging and anticancer treatments. The study of the antioxidation protection in D. radiodurans is therefore of considerable potential interest for medicine and public health.

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Section: Stress Response Transcriptional Regulatorsmentioning

confidence: 99%

Oxidative Stress Resistance inDeinococcus radiodurans

Slade

Radman

2011

Microbiol Mol Biol Rev

648

639

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“…PprI consists of an N-terminal zinc peptidase-like domain, a helix-turn-helix motif, and a C-terminal GAF-like sensory domain. Although a missense mutation in the C-terminal domain of D. deserti PprI substantially diminishes the radioresistance, the role of the C-terminal domain is largely unknown [71]. D. radiodurans PprI upregulates 31 proteins and downregulates 4 proteins following 1-kGy irradiation [72].…”

Section: Stress Response In D Radioduransmentioning

confidence: 99%

DNA repair in hyperthermophilic and hyperradioresistant microorganisms

Ishino

Narumi

2015

Current Opinion in Microbiology

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“…In D. radiodurans, radiation tolerance and DNA damage-induced expression of recA requires the presence of irrE (Earl et al, 2002a;Hua et al, 2003), encoding a Deinococcus-specific regulator protein (de Groot et al, 2009;Vujicic-Zagar et al, 2009). A D. deserti DirrE mutant, which grows normally under standard conditions, is extremely sensitive to radiation (Fig.…”

Section: Each Single Reca Mutant Is As Uv and Gamma Radiation-resistamentioning

confidence: 99%

“…D. deserti was grown at 30°C in 10-fold diluted tryptic soy broth (TSB/10) supplemented with trace elements (Vujicic-Zagar et al, 2009). Antibiotics were used at the following concentrations for D. deserti: streptomycin, 10 mg ml -1 ; kanamycin, 10 mg ml -1 ; chloramphenicol, 3 mg ml -1 ; rifampicin, 10 mg ml -1 .…”

Section: Bacterial Strains Plasmids and Growth Conditionsmentioning

confidence: 99%

“…The products of additional genes specifically conserved in Deinococcus are also involved in DNA repair and radiation tolerance. These include PprA (reported to stimulate ligase activity) (Narumi et al, 2004), DdrA (an oligomeric ring-forming protein involved in DNA extremity protection) (Harris et al, 2004;Gutsche et al, 2008), DdrB, DdrC and DdrD (functions unknown) de Groot et al, 2009) and IrrE (regulator of recA and pprA expression) (Earl et al, 2002a;Hua et al, 2003;Lu et al, 2009;Vujicic-Zagar et al, 2009). Homologues of DNA repair photolyases and specialized translesion synthesis (TLS) DNA polymerases have not been identified in D. radiodurans and D. geothermalis.…”

Section: Introductionmentioning

confidence: 99%

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Mutagenic lesion bypass and two functionally different RecA proteins in Deinococcus deserti

Dulermo

Fochesato

Blanchard

et al. 2009

Molecular Microbiology

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SummaryRecA is essential for extreme radiation tolerance in Deinococcus radiodurans. Interestingly, Sahara bacterium Deinococcus deserti has three recA genes (recAC, recAP1, recAP3) that code for two different RecA proteins (RecAC, RecAP). Moreover, and in contrast to other sequenced Deinococcus species, D. deserti possesses homologues of translesion synthesis (TLS) DNA polymerases, including ImuY and DnaE2. Together with a lexA homologue, imuY and dnaE2 form a gene cluster similar to a widespread RecA/LexA-controlled mutagenesis cassette. After having developed genetic tools, we have constructed mutant strains to characterize these recA and TLS polymerase genes in D. deserti. Both RecAC and RecAP are functional and allow D. deserti to survive, and thus repair massive DNA damage, after exposure to high doses of radiation. D. deserti is mutable by UV, which requires ImuY, DnaE2 and RecAC, but not RecAP. RecAC, but not RecAP, facilitates induced expression of imuY and dnaE2 following UV exposure. We propose that the extra recAP1 and recAP3 genes may provide higher levels of RecA protein for efficient error-free repair of DNA damage, without further increasing error-prone lesion bypass by ImuY and DnaE2, whereas limited TLS may contribute to adaptation to harsh conditions by generating genetic variability.

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Crystal Structure of the IrrE Protein, a Central Regulator of DNA Damage Repair in Deinococcaceae

Cited by 73 publications

References 51 publications

Oxidative Stress Resistance inDeinococcus radiodurans

Oxidative Stress Resistance inDeinococcus radiodurans

DNA repair in hyperthermophilic and hyperradioresistant microorganisms

Mutagenic lesion bypass and two functionally different RecA proteins in Deinococcus deserti

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