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TheEscherichia coli β sliding clamp protein is proposed to play an important role in effecting switches between different DNA polymerases during replication, repair, and translesion DNA synthesis. We recently described how strains bearing thednaN159 allele, which encodes a mutant form of the β clamp (β159), display a UV-sensitive phenotype that is suppressed by inactivation of DNA polymerase IV (M. D. Sutton, J. Bacteriol. 186:6738-6748, 2004). As part of an ongoing effort to understand mechanisms of DNA polymerase management inE. coli , we have further characterized effects of thednaN159 allele on polymerase usage. Three of the fiveE.coli DNA polymerases (II, IV, and V) are regulated as part of the global SOS response. Our results indicate that elevated expression of thedinB -encoded polymerase IV is sufficient to result in conditional lethality of thednaN159 strain. In contrast, chronically activated RecA protein, expressed from therecA730 allele, is lethal to thednaN159 strain, and this lethality is suppressed by mutations that either mitigate RecA730 activity (i.e., ΔrecR ), or impair the activities of DNA polymerase II or DNA polymerase V (i.e., ΔpolB or ΔumuDC ). Thus, we have identified distinct genetic requirements whereby each of the three different SOS-regulated DNA polymerases are able to confer lethality upon thednaN159 strain, suggesting the presence of multiple mechanisms by which the actions of the cell's different DNA polymerases are managed in vivo.

Roles of the Escherichia coli RecA Protein and the Global SOS Response in Effecting DNA Polymerase Selection In Vivo