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Nucleic Acids Research, 1994, Vol. 22, No. 24 5177-5183
© 1994

Articles

Family A and family B DNA polymerases are structurally related: evolutionary implications

Weiguo Zhu and Junetsu Ito*

Department of Microbiology and Immunology, College of Medicine, The University of Arizona Tucson, AZ 85724, USA

*To whom correspondence should be addressed

Received October 15, 1994. Accepted October 27, 1994.

In order to establish the evolutionary relationship between the family A and B DNA polymerases, we have closely compared the 3'-> 5' exonuclease domains between the Klenow fragment of E.coll DNA polymerase I (a family A DNA polymerase) and the bacterlophage PRD1 DNA polymerase, the smallest member of the DNA polymerase family B. Although the PRD1 DNA polymerase has a smaller 3'-> 5' exonuclease domain, its active sites appear to be very similar to those of the Klenow fragment. Site-directed mutagenesis studies revealed that the residues important for the 3'-> 5' exonuclease activity, particularly metal binding ligands for the Klenow fragment, are all conserved In the PRD1 DNA polymerase as well. The metal binding ligands are also essential for the strand-displacement activity of the PRD1 DNA polymerase. Based on these results and the studies by others in various systems, we conclude that family A and B DNA polymerases, at least in the 3' -> 5' exonuclease domain, are structurally as well as evolutionarily related.


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