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A Model for the structure of the ${it Escherichia coli}$ SOS-regulated UmuD$$_{2}$$ protein

Sutton, M. D.*; Guzzo, A.*; Narumi, Issei; Costanzo, M.*; Altenbach, C.*; Ferentz, A. E.*; Hubbell, W. L.*; Walker, G. C.*

UmuD$$_{2}$$ protein is a regulatory subunit of ${it Escherichia coli}$ DNA polymerase V. This protein forms a complex with UmuC protein, a catalytic subunit of DNA polymerase V, and plays a important role in error-prone translesion DNA synthesis, which serves as the mechanistic basis for most DNA-damaging agent and UV light mutagenesis. In this paper, based on the results of a combination of experimental studies, we have developed a refined model for the structure of the UmuD$$_{2}$$ homodimer. Implications of the structural change of UmuD$$_{2}$$ protein with respect to its roles in managing the action of DNA polymease V are discussed.

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