title: DNA polymerase V kinetics support the instructive nature of an oxidized abasic lesion in Escherichia coli.
abstract: Translesion synthesis past an oxidized abasic site, 2-deoxyribonolactone, in Escherichia coli results in high levels of dG incorporation and is dependent upon DNA polymerase V (Pol V). Kinetic experiments performed here affirm that Pol V preferentially incorporates dG opposite 2-deoxyribonolactone (L). Pol V discriminates between dG and dA on the basis of the apparent KD, suggesting that L provides instructive structural information to the enzyme despite lacking a Watson-Crick base.
authors.affiliation: Department of Chemistry, Johns Hopkins University , 3400 North Charles Street, Baltimore, Maryland 21218, United States.
authors.forename: John Ernest V
authors.initials: JE
authors.lastname: Bajacan
authors.forename: Marc M
authors.initials: MM
authors.lastname: Greenberg
mesh_terms: D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D003848:Deoxyguanine Nucleotides / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D013400:Sugar Acids / Q000737:chemistry
chemical_list: D003848:Deoxyguanine Nucleotides; D029968:Escherichia coli Proteins; D013400:Sugar Acids; C056405:2,4,5-trihydroxypentanoic acid gamma-lactone; C120926:DNA polymerase V, E coli; D004259:DNA-Directed DNA Polymerase