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Nucleic Acids Research, 1988, Vol. 16, No. 16 7961-7973
© 1988

Articles

The evolutionary conservation of DNA polymerase {alpha}

Mitchell A. Miller, David Korn and Teresa S.-F. Wang*

Laboratory of Experimental Oncology, Department of Pathology, Stanford University School of Medicine, Stanford University Stanford, CA 94305, USA

*To whom correspondence should be addressed

Received April 26, 1988. Accepted June 11, 1988.

The evolutionary conservation of DNA polymerase {alpha} was assessed by immunological and molecular genetic approachea. Four anti-human KB cell DNA polymerase a monoclonal antibodies were teated for their ability to recognize a phylogenetically broad array of eukaryotic DNA polymerases. While the aingle non-neutralizing antibody used in thia study recognizes higher mammalian (human, simian, canine, and bovine) polymerases only, three neutralizing antibodies exhibit greater, but variable, extents of cross-reactivity among vertebrate species. The most highly cross-reactive antibody recognizes a unique epitope on a 165–180 kDa catalytic polypeptide in cell lysates from several eukaryotic sources, as distant from man as the smphibiana. Genomic Southern hybridization studies with the cDNA of the human DNA polymerase {alpha} catalytic polypeptide identify the existence of many consensus DNA sequences within the DNA polymerase genes of vertebrate, invertebrate, plant and unicellular organisms. These findings illustrate the differential evolutionary conservation of four unique epitopes on DNA polymerase {alpha} among vertebrates and the conservation of specific genetic sequences, presumably reflective of critical functional domains, in the DNA polymerase genes from a broad diversity of living forms.


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