Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/39350
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Título : A general structure for DNA-dependent DNA polymerases
Autor : Blanco, Luis, Bernad, Antonio, Blasco, María A., Salas, Margarita
Palabras clave : DNA polymerase
3′–5′ exonuclease
Sequence homology
Phage φ29
Site-directed mutagenesis
Fecha de publicación : Apr-1991
Editor: Elsevier
Citación : Gene 100: 27-38 (1984)
Resumen: In addition to the general 3′–5′ exonuclease domain described by Bernad et al. [Cell 59 (1989) 219–228] significant amino acid (aa) sequence similarity has been found in the C-terminal portion of 27 DNA-dependent DNA polymerases belonging to the two main superfamilies : (i) Escherichia coli DNA polymerase I (Poll)-like prokaryotic DNA polymerases, and (i) DNA polymerase α-like prokaryotic and eukaryotic (viral and cellular) DNA polymerases. The six most conserved C-terminal regions, spanning approx. 340 aa, are located in the same linear arrangement and contain highly conserved motifs and critical residues involved in the polymerization function. According to the three-dimensional model of PolIk (Klenow fragment), these six conserved regions are located in the proposed polymerization domain, forming the metal and dNTP binding sites and the cleft for holding the DNA template. Site-directed mutagenesis in the φ29 DNA polymerase supports some of these structural predictions. Therefore, it is likely that a ‘Klenow-like core’, containing the DNA polymerase and 3′–5′ exonuclease activities, has evolved from a common ancestor, giving rise to the present-day prokaryotic and eukaryotic DNA polymerases.
Versión del editor: http://dx.doi.org/10.1016/0378-1119(91)90346-D
URI : http://hdl.handle.net/10261/39350
ISSN: 0378-1119
DOI: 10.1016/0378-1119(91)90346-D
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