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- W4301321736 abstract "Escherichia coli DNA polymerase V (pol V), a heterotrimeric complex composed of UmuD'2C, is marginally active. ATP and RecA play essential roles in the activation of pol V for DNA synthesis including translesion synthesis (TLS). We have established three features of the roles of ATP and RecA. 1) RecA-activated DNA polymerase V (pol V Mut), is a DNA-dependent ATPase; 2) bound ATP is required for DNA synthesis; 3) pol V Mut function is regulated by ATP, with ATP required to bind primer/template (p/t) DNA and ATP hydrolysis triggering dissociation from the DNA. Pol V Mut formed with an ATPase-deficient RecA E38K/K72R mutant hydrolyzes ATP rapidly, establishing the DNA-dependent ATPase as an intrinsic property of pol V Mut distinct from the ATP hydrolytic activity of RecA when bound to single-stranded (ss)DNA as a nucleoprotein filament (RecA*). No similar ATPase activity or autoregulatory mechanism has previously been found for a DNA polymerase." @default.
- W4301321736 created "2022-10-05" @default.
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- W4301321736 date "2014-04-01" @default.
- W4301321736 modified "2023-09-27" @default.
- W4301321736 title "DNA polymerase V activity is autoregulated by a novel intrinsic DNA-dependent ATPase" @default.
- W4301321736 doi "https://doi.org/10.48550/arxiv.1404.0307" @default.
- W4301321736 hasPublicationYear "2014" @default.
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