期刊
NATURE
卷 460, 期 7253, 页码 359-363出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nature08178
关键词
-
资金
- National Institutes of Health [ES12259, R37GM21422, GM32335]
- NICHD/NIH
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 39-end to free polV (UmuD'C-2) to form an active mutasome (polV Mut) with the composition UmuD'C-2-RecA-ATP. PolV 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 polV 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.
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