English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/39852
Title: A conserved 3′→5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases
Authors: Bernad, Antonio; Blanco, Luis; Lázaro, José M.; Martín, Gil; Salas, Margarita
Issue Date: 6-Oct-1989
Publisher: Elsevier
Citation: Cell 59(1): 219-228 (1989)
Abstract: The 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
URI: http://hdl.handle.net/10261/39852
DOI: 10.1016/0092-8674(89)90883-0
ISSN: 0092-8674
E-ISSN: 1097-4172
Appears in Collections:(CBM) Artículos
Files in This Item:
There are no files associated with this item.
Show full item record

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.