Redox controls RecA protein activity via reversible oxidation of its methionine residues

Henry, Camille; Loiseau, Laurent; Vergnes, Alexandra; Vertommen, Didier; Mérida-Floriano, Ángela; Chitteni-Pattu, Sindhu; Wood, Elizabeth A.; Casadesús, Josep; Cox, Michael M.; Barras, Frédéric; Ezraty, Benjamin

doi:10.7554/elife.63747

Cited by 19 publications

(15 citation statements)

References 48 publications

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“…The SOS system also includes other features, such as the induction of bypass polymerases, that carry the cost of elevated mutagenesis (Gonzalez & Woodgate, 2002) and therefore seem suited to be last‐ditch response to damage. A recent study provided indirect evidence that the SOS‐controlled UvrABC complex, which is known to remove bulky DNA lesions, may also play a role in removing oxidative lesions (Henry et al., 2021). An interesting possibility is that oxidative stress comprises the most common SOS trigger in the lives of bacteria.…”

Section: Discussionmentioning

confidence: 99%

Escherichia coli induces DNA repair enzymes to protect itself from low‐grade hydrogen peroxide stress

Gupta

Imlay

2022

Molecular Microbiology

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Escherichia coli responds to hydrogen peroxide (H2O2) by inducing defenses that protect H2O2‐sensitive enzymes. DNA is believed to be another important target of oxidation, and E. coli contains enzymes that can repair oxidative lesions in vitro. However, those enzymes are not known to be induced by H2O2, and experiments have indicated that they are not necessary for the cell to withstand natural (low‐micromolar) concentrations. In this study, we used H2O2‐scavenging mutants to impose controlled doses of H2O2 for extended time. Transcriptomic analysis revealed that in the presence of 1 µM cytoplasmic H2O2, the OxyR transcription factor‐induced xthA, encoding exonuclease III. The xthA mutants survived a conventional 15‐min exposure to even 100 times this level of H2O2. However, when these mutants were exposed to 1 µM H2O2 for hours, they accumulated DNA lesions, failed to propagate, and eventually died. Although endonuclease III (nth) was not induced, nth mutants struggled to grow. Low‐grade H2O2 stress also activated the SOS regulon, and when this induction was blocked, cell replication stopped. Collectively, these data indicate that physiological levels of H2O2 are a real threat to DNA, and the engagement of the base‐excision‐repair and SOS systems is necessary to enable propagation during protracted stress.

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Section: Discussionmentioning

confidence: 99%

Escherichia coli induces DNA repair enzymes to protect itself from low‐grade hydrogen peroxide stress

Gupta

Imlay

2022

Molecular Microbiology

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“…Under high H 2 O 2 levels, the Mets in E. coli RecA may be oxidized to MetSO, losing function. MsrA/B are required for maintaining the recombinase function of RecA under oxidative stress ( 50 ). These findings imply that the regulation of oxidized protein repair involves cross talk with the DNA repair signaling pathway in D. radiodurans .…”

Section: Discussionmentioning

confidence: 99%

A Novel Small RNA, DsrO, in Deinococcus radiodurans Promotes Methionine Sulfoxide Reductase ( msrA ) Expression for Oxidative Stress Adaptation

Chen

Zhao

Lin

et al. 2022

Appl Environ Microbiol

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“…These two residues are not conserved in PaRecA and DrRecA originating from bacteria that are highly resistant to oxidative stress (Fig. 2 ) 41 .…”

Section: Discussionmentioning

confidence: 99%

Design and comparative characterization of RecA variants

Val

Nasser

Abaibou

et al. 2021

Sci Rep

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RecA plays a central role in DNA repair and is a main actor involved in recombination and activation of the SOS response. It is also used in the context of biotechnological applications in recombinase polymerase isothermal amplification (RPA). In this work, we studied the biological properties of seven RecA variants, in particular their recombinogenic activity and their ability to induce the SOS response, to better understand the structure–function relationship of RecA and the effect of combined mutations. We also investigated the biochemical properties of RecA variants that may be useful for the development of biotechnological applications. We showed that Dickeya dadantii RecA (DdRecA) had an optimum strand exchange activity at 30 °C and in the presence of a dNTP mixture that inhibited Escherichia coli RecA (EcRecA). The differences between the CTD and C-tail of the EcRecA and DdRecA domains could explain the altered behaviour of DdRecA. D. radiodurans RecA (DrRecA) was unable to perform recombination and activation of the SOS response in an E. coli context, probably due to its inability to interact with E. coli recombination accessory proteins and SOS LexA repressor. DrRecA strand exchange activity was totally inhibited in the presence of chloride ions but worked well in acetate buffer. The overproduction of Pseudomonas aeruginosa RecA (PaRecA) in an E. coli context was responsible for a higher SOS response and defects in cellular growth. PaRecA was less inhibited by the dNTP mixture than EcRecA. Finally, the study of three variants, namely, EcPa, EcRecAV1 and EcRecAV2, that contained a combination of mutations that, taken independently, are described as improving recombination, led us to raise new hypotheses on the structure–function relationship and on the monomer–monomer interactions that perturb the activity of the protein as a whole.

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Redox controls RecA protein activity via reversible oxidation of its methionine residues

Cited by 19 publications

References 48 publications

Escherichia coli induces DNA repair enzymes to protect itself from low‐grade hydrogen peroxide stress

Escherichia coli induces DNA repair enzymes to protect itself from low‐grade hydrogen peroxide stress

A Novel Small RNA, DsrO, in Deinococcus radiodurans Promotes Methionine Sulfoxide Reductase ( msrA ) Expression for Oxidative Stress Adaptation

Design and comparative characterization of RecA variants

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