DNA polymerase V activity is autoregulated by a novel intrinsic DNA-dependent ATPase

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. (...

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Published in:eLife 2014-04, Vol.3, p.e02384-e02384
Main Authors: Erdem, Aysen L, Jaszczur, Malgorzata, Bertram, Jeffrey G, Woodgate, Roger, Cox, Michael M, Goodman, Myron F
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Anisotropy
ATPase
Biochemistry
Deoxyribonucleic acid
DNA
DNA biosynthesis
DNA polymerase V
DNA, Single-Stranded - genetics
DNA, Single-Stranded - metabolism
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
DNA-directed DNA polymerase
DNA-Directed DNA Polymerase - genetics
DNA-Directed DNA Polymerase - metabolism
Enzymes
Escherichia coli - genetics
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Gene Expression Regulation, Bacterial
Hydrolysis
Mutation
Nucleoproteins - genetics
Nucleoproteins - metabolism
pol V Mut
Rec A Recombinases - genetics
Rec A Recombinases - metabolism
RecA
RecA protein
Single-stranded DNA
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Summary: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.DOI: http://dx.doi.org/10.7554/eLife.02384.001.
ISSN:2050-084X
2050-084X
DOI:10.7554/elife.02384