Activation of phenotypic subpopulations in response to ciprofloxacin
                    treatment in Acinetobacter baumannii

MacGuire, Ashley Erin

doi:10.17760/d20003082

Cited by 1 publication

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“…It is conceivable that in processes as diverse as the DNA damage response, the stepwise evolution of high quinolone resistance, and prophage induction are too complex to be regulated by a single transcription factor, albeit triggered by the same mechanism. The data presented here support the idea that the regulation of the DNA damage response across bacteria includes more than the archetype LexA/phage regulators/RecA (28,29). We propose that small proteins, like gp7 and DdrR, are widespread in bacteria and act as accessory factors to regulatory proteins that undergo RecA*-mediated self-cleavage, like LexA, UmuDAb and phage regulators.…”

Section: Discussionsupporting

confidence: 81%

The Small DdrR Protein Directly Interacts with the UmuDAb Regulator of the Mutagenic DNA Damage Response in Acinetobacter baumannii

et al. 2022

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Acinetobacter baumannii poses a great threat in healthcare settings worldwide with clinical isolates displaying an ever-evolving multidrug-resistance. In strains of A. baumannii , expression of multiple error-prone polymerase genes is co-repressed by UmuDAb, a member of the LexA superfamily, and a small protein, DdrR. It is currently unknown how DdrR establishes this repression. Here, we use surface plasmon resonance spectrometry to show that DdrR forms a stable complex with the UmuDAb regulator. Our results indicate that the carboxy-terminal dimerization domain of UmuDAb forms the interaction interface with DdrR. Our in vitro data also show that RecA-mediated inactivation of UmuDAb is inhibited when this transcription factor is bound to its target DNA. In addition, we show that DdrR interacts with a putative prophage repressor, homologous to LexA superfamily proteins. These data suggest that DdrR modulates DNA damage response and prophage induction in A. baumannii by binding to LexA-like regulators. Importance We previously identified a 50-residue bacteriophage protein, gp7, which interacts with and modulates the function of the LexA transcription factor from Bacillus thuringiensis . Here we present data that indicates that the small DdrR protein from A. baumannii likely coordinates the SOS response and prophage processes by also interacting with LexA superfamily members. We suggest that similar small proteins that interact with LexA-like proteins to coordinate DNA repair and bacteriophage functions may be common to many bacteria that mount the SOS response.

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Section: Discussionsupporting

confidence: 81%