The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis.


In Escherichia coli, the dinB gene is required for the SOS-induced lambda untargeted mutagenesis pathway and confers a mutator phenotype to the cell when the gene product is overexpressed. Here, we report that the purified DinB protein is a DNA polymerase. This novel E. coli DNA polymerase (pol IV) is shown to be strictly distributive, devoid of proofreading activity, and prone to elongate bulged (misaligned) primer/template structures. Site-directed mutagenesis experiments of dinB also demonstrate that the polymerase activity of DinB is required for its in vivo mutagenicity. Along with the sequence homologies previously found within the UmuC-like protein family, these results indicate that the uncovered DNA polymerase activity may be a common feature of all these homologous proteins.



Historical Protein Properties (MW, pI, ...), Exonuclease Activity, Nucleotide Incorporation, Mutational Analysis


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Polymerase Reference Property Result Context
Eco Pol IV Wagner JE1999 Molecular Weight 3.2E+04 Dalton Technique: Gel Filtration
Eco Pol IV Wagner JE1999 3-5' Exonuclease (proofreading) No
Eco Pol IV Wagner JE1999 Cloned or native Cloned in E. coli
Eco Pol IV Wagner JE1999 Tagged Yes
Eco Pol IV Wagner JE1999 Tag Name His tag
Eco Pol IV Wagner JE1999 Full length or truncated Full length
Eco Pol IV Wagner JE1999 Processivity 1bp
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