2024-03-29T13:14:11Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/398522018-10-17T08:28:29Zcom_10261_79com_10261_1col_10261_332
A conserved 3′→5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases
Bernad, Antonio
Blanco, Luis
Lázaro, José M.
Martín, Gil
Salas, Margarita
National Institutes of Health (US)
Ministerio de Economía y Competitividad (España)
Instituto de Salud Carlos III
Fundación Ramón Areces
Consejo Superior de Investigaciones Científicas (España)
Caja de Ahorros y Monte de Piedad de Madrid
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.
2011-09-22T11:15:59Z
2011-09-22T11:15:59Z
1989-10-06
artículo
Cell 59(1): 219-228 (1989)
0092-8674
http://hdl.handle.net/10261/39852
10.1016/0092-8674(89)90883-0
1097-4172
http://dx.doi.org/10.13039/100000002
http://dx.doi.org/10.13039/501100003329
http://dx.doi.org/10.13039/100008054
http://dx.doi.org/10.13039/501100003339
http://dx.doi.org/10.13039/501100004587
eng
http://dx.doi.org/10.1016/0092-8674(89)90883-0
closedAccess
Elsevier