PMID:12497
| Citation |
Kelly, WS and Grindley, ND (1976) polA6, A mutation affecting the DNA binding capacity of DNA polymerase I. Nucleic Acids Res. 3:2971-84 |
|---|---|
| Abstract |
The polA6 mutation is an allele of the polA gene of Escherichia coli which produces a DNA polymerase I species readily distinguishable from that produced by the wild type allele. Experiments described here show that this enzyme has an altered pH optimum for polymerization and a lower binding affinity for DNA. The defect clearly lies within the carboxyl-terminal large fragment of the enzyme produced by in vivo or in vitro proteolysis since the fragment has the same pH optimum for polymerization as the intact enzyme. The polA6 enzyme and its fragment are more sensitive to phosphate ions than the wild type polymerase, and the large fragment is less efficient at binding poly d(AT) in in vitro binding assays. Although the specific nucleolytic activity of the polA6 enzyme is higher than that of the wild type, there is no apparent alteration in pH optimum for the hydrolysis of eigher double or single stranded DNA. |
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| Keywords |
Alleles; Binding Sites; DNA Polymerase I/isolation & purification; DNA Polymerase I/metabolism; DNA, Bacterial; DNA-Directed DNA Polymerase/metabolism; Escherichia coli/enzymology; Genes; Hydrogen-Ion Concentration; Kinetics; Mutation; Protein Binding |
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