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Nucleic Acids Research, 1987, Vol. 15, No. 22 9299-9308
© 1987

Articles

Autoantibody to the proliferating cell nuclear antigen neutralizes the activity of the auxiliary protein for DNA polymerase delta

Cheng-Keat Tan, Kevin Sullivan1, Xiangyang Li, Eng M. Tan1, Kathleen M. Downey and Antero G. So

Department of Medicine, Department of Biochemistry and Molecular Biology and Center for Blood Diseases, University of Miami School of Medicine Miami, FL 33101 1The W.M.Keck Foundation Autoimmune Disease Center, Scripps Clinic and Research Foundation La Jolla, CA 92037, USA

Received August 14, 1987. Revised October 9, 1987. Accepted October 9, 1987.

Two murine monoclonal antibodies to the proliferating cell nuclear antigen (PCNA), a rabbit anti-N-terminal peptide antibody and human autoantibody to PCNA reacted with the auxiliary protein for DNA polymerase delta from fetal calf thymus following SDS-polyacrylamide gel electrophoresis, confirming the identity of PCNA and the auxiliary protein. Undenatured auxiliary protein was immunoprecipitated by the human autoantibody, but not by the monoclonal antibodies, which were raised to SDS-denatured PCNA, nor by the anti-N-terminal peptide antibody, suggesting that the epitopes recognized by both the monoclonal antibodies and the anti-peptide antibody are not exposed in the native protein. The human anti-PCNA autoantibody neutralized the activity of the auxiliary protein for DNA polymerase delta, but did not inhibit the activity of pol delta itself. The ability of pol delta to utilize template/primers containing long stretches of single- stranded template was inhibited by the anti-PCNA autoantibody, whereas the activity of pol alpha on such templatea was not affected, confirming the specificity of the auxiliary protein for pol delta. The ability of PCNA, a cell cycle-regulated protein, to regulate the activity of pol delta suggests a central role for pol delta in cellular DNA replication.


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