The active form of DNA polymerase V is UmuD'(2)C-RecA-ATP.

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'(2)C) to form an active mutasome (pol V Mut) with the composition UmuD'(2)C-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*.

SUBMITTER: Jiang Q 

PROVIDER: S-EPMC2731490 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature