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A conserved 3′→5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases

AuthorsBernad, Antonio; Blanco, Luis ; Lázaro, José M. ; Martín, Gil; Salas, Margarita
Issue Date6-Oct-1989
CitationCell 59(1): 219-228 (1989)
AbstractThe 3′→5′ exonuclease active site of E. coli DNA polymerase I is predicted to be conserved for both prokaryotic and eukaryotic DNA polymerases based on amino acid sequence homology. Three amino acid regions containing the critical residues in the E. coli DNA polymerase I involved in metal binding, single-stranded DNA binding, and catalysis of the exonuclease reaction are located in the amino-terminal half and in the same linear arrangement in several prokaryotic and eukaryotic DNA polymerases. Site-directed mutagenesis at the predicted exonuclease active site of the ϕ29 DNA polymerase, a model enzyme for prokaryotic and eukaryotic α-like DNA polymerases, specifically inactivated the 3′→5′ exonuclease activity of the enzyme. These results reflect a high evolutionary conservation of this catalytic domain. Based on structural and functional data, a modular organization of enzymatic activities in prokaryotic and eukaryotic DNA polymerases is also proposed.
Publisher version (URL)http://dx.doi.org/10.1016/0092-8674(89)90883-0
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