The active form of DNA polymerase V is UmuD′2C–RecA–ATP

Qingfei Jiang, Kiyonobu Karata, Roger Woodgate, Michael M. Cox and Myron F. Goodman ()
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Qingfei Jiang: University of Southern California, University Park, Los Angeles, California 90089-2910, USA
Kiyonobu Karata: Laboratory of Genomic Integrity, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-3371, USA
Roger Woodgate: Laboratory of Genomic Integrity, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-3371, USA
Michael M. Cox: University of Wisconsin-Madison, Madison, Wisconsin 53706, USA
Myron F. Goodman: University of Southern California, University Park, Los Angeles, California 90089-2910, USA

Nature, 2009, vol. 460, issue 7253, 359-363

Abstract: Abstract DNA-damage-induced SOS mutations arise when Escherichia coli DNA polymerase (pol) V, activated by a RecA nucleoprotein filament (RecA*), catalyses translesion DNA synthesis. Here we address two longstanding enigmatic aspects of SOS mutagenesis, the molecular composition of mutagenically active pol V and the role of RecA*. We show that RecA* transfers a single RecA–ATP stoichiometrically from its DNA 3′-end to free pol V (UmuD′2C) to form an active mutasome (pol V Mut) with the composition UmuD′2C–RecA–ATP. Pol V Mut catalyses TLS in the absence of RecA* and deactivates rapidly upon dissociation from DNA. Deactivation occurs more slowly in the absence of DNA synthesis, while retaining RecA–ATP in the complex. Reactivation of pol V Mut is triggered by replacement of RecA–ATP from RecA*. Thus, the principal role of RecA* in SOS mutagenesis is to transfer RecA–ATP to pol V, and thus generate active mutasomal complex for translesion synthesis.

Date: 2009
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DOI: 10.1038/nature08178

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