ArticleNucleic acids research2012
Selective disruption of the DNA polymerase III α-β complex by the umuD gene products.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- The SOS system: A complex and tightly regulated response to DNA damage.Environmental and molecular mutagenesis · 2019Review
- Altering the N-terminal arms of the polymerase manager protein UmuD modulates protein interactions.PloS one · 2017Article
- Comprehensive Analysis of DWARF14-LIKE2 (DLK2) Reveals Its Functional Divergence from Strigolactone-Related Paralogs.Frontiers in plant science · 2017Article
- The β2 clamp in the Mycobacterium tuberculosis DNA polymerase III αβ2ε replicase promotes polymerization and reduces exonuclease activity.Scientific reports · 2016Article
- P1 Ref Endonuclease: A Molecular Mechanism for Phage-Enhanced Antibiotic Lethality.PLoS genetics · 2016Article
- Polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.Nucleic acids research · 2013Article
- The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the β-clamp processivity factor.BMC structural biology · 2013Article
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Authors and funding
4 authors.
Funding
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Abstract
DNA polymerase III (DNA pol III) efficiently replicates the Escherichia coli genome, but it cannot bypass DNA damage. Instead, translesion synthesis (TLS) DNA polymerases are employed to replicate past damaged DNA; however, the exchange of replicative for TLS polymerases is not understood. The umuD gene products, which are up-regulated during the SOS response, were previously shown to bind to the α, β and ε subunits of DNA pol III. Full-length UmuD inhibits DNA replication and prevents mutagenic TLS, while the cleaved form UmuD' facilitates mutagenesis. We show that α possesses two UmuD binding sites: at the N-terminus (residues 1-280) and the C-terminus (residues 956-975). The C-terminal site favors UmuD over UmuD'. We also find that UmuD, but not UmuD', disrupts the α-β complex. We propose that the interaction between α and UmuD contributes to the transition between replicative and TLS polymerases by removing α from the β clamp.
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