title: Properties of the Escherichia coli in DNA binding (unwinding) protein: interaction with DNA polymerase and DNA.
abstract: The E. coli DNA binding protein reduces the activity of the single-strand-specific nucleases associated with all three DNA polymerases known in E. coli. A slight excess of binding protein over that required to saturate the DNA template leads to total inhibition of activity of the 3' --> 5' nucleases associated with DNA polymerases I and III, but restores maximum activity of the DNA polymerase II-associated nuclease. The binding protein forms a specific complex with DNA polymerase II in the absence of DNA, and it is this complex that degrades a DNA.binding protein complex. Binding protein also facilitates the binding of DNA polymerase II to single-stranded DNA, whereas the binding to DNA of DNA polymerase I is inhibited. These data may explain the specificity with which the binding protein enhances the synthetic ability of DNA polymerase II.
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D002417:Cattle; D002499:Centrifugation, Density Gradient; D004247:DNA / Q000378:metabolism*; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D001426:Bacterial Proteins; D004277:DNA, Single-Stranded; D004247:DNA; D004254:DNA Nucleotidyltransferases