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After DNA damage, the multi-drug resistant pathogen Acinetobacter baumannii activates its SOS response, possibly allowing mutagenesis to occur by inducing multiple errorprone polymerases. A. baumannii uses the non-canonical repressor protein UmuDAb to repress operons of these polymerases. It has an N-terminal domain (NTD) with 2 helices (HTH1 & HTH2) whose sequences are needed for repression1. Like other bacterial SOS repressors such as LexA, UmuDAb dimerizes. BACTH analyses2 showed that UmuDAb forms dimers via its LexA-like G124 residue and UmuD-like N100 residue (UmuD is a component of an error-prone polymerase). However, N100 is not needed if the C termini are free. The C-terminal 12 amino acids (which include W192 and R201) of UmuDAb are also required to form dimers.

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Repressor of the SOS Response Mechanism in Acinetobacter baumannii requires Helix-Formation and Dimerization for its DNA-binding Ability



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