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A model for SOS-lesion-targeted mutations in Escherichia coli

Author

Listed:
  • Phuong Pham

    (Hedco Molecular Biology Laboratories, University of Southern California)

  • Jeffrey G. Bertram

    (Hedco Molecular Biology Laboratories, University of Southern California)

  • Mike O'Donnell

    (Rockefeller University and Howard Hughes Medical Institute)

  • Roger Woodgate

    (Section on DNA Replication, Repair and Mutagenesis, National Institute of Child Health and Human Development, National Institutes of Health)

  • Myron F. Goodman

    (Hedco Molecular Biology Laboratories, University of Southern California)

Abstract

The UmuD′2C protein complex (Escherichia coli pol V)1,2,3 is a low-fidelity DNA polymerase (pol) that copies damaged DNA in the presence of RecA, single-stranded-DNA binding protein (SSB) and the β,γ-processivity complex of E. coli pol III (ref. 4). Here we propose a model to explain SOS-lesion-targeted mutagenesis, assigning specific biochemical functions for each protein during translesion synthesis. (SOS lesion-targeted mutagenesis occurs when pol V is induced as part of the SOS response to DNA damage and incorrectly incorporates nucleotides opposite template lesions.) Pol V plus SSB catalyses RecA filament disassembly in the 3′ to 5′ direction on the template, ahead of the polymerase, in a reaction that does not involve ATP hydrolysis. Concurrent ATP-hydrolysis-driven filament disassembly in the 5′ to 3′ direction results in a bidirectional stripping of RecA from the template strand. The bidirectional collapse of the RecA filament restricts DNA synthesis by pol V to template sites that are proximal to the lesion, thereby minimizing the occurrence of untargeted mutations at undamaged template sites.

Suggested Citation

  • Phuong Pham & Jeffrey G. Bertram & Mike O'Donnell & Roger Woodgate & Myron F. Goodman, 2001. "A model for SOS-lesion-targeted mutations in Escherichia coli," Nature, Nature, vol. 409(6818), pages 366-370, January.
    • Handle: RePEc:nat:nature:v:409:y:2001:i:6818:d:10.1038_35053116
    DOI: 10.1038/35053116
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