Date of Award:

5-1-1988

Document Type:

Dissertation

Degree Name:

Doctor of Philosophy (PhD)

Department:

Biology

Department name when degree awarded

Biology/Molecular Biology

Committee Chair(s)

Joseph K. K. Li

Committee

Joseph K. K. Li

Committee

Jon Y. Takenoto

Committee

Dennis L. Welker

Committee

Jeffery K. Kondo

Committee

Bruce R. Copeland

Abstract

Cells infected with Epstein-Barr virus (EBV) express a DNA polymerase that is distinguishable from the host DNA polymerases. The amino acid sequence encoded by the BALF5 open-reading frame (ORF) of the EBV genome was found to contain regions of strong similarity to the amino acid sequence of the herpes simplex (HSV-1) DNA polymerase. The putative amino acid sequence of BALF5 contains a potential 'leucine zipper' DNA binding domain. The BALF5 ORF was expressed in Escherichia coli using a pUC19 vector. The expressed DNA polymerase activity could be neutralized using EBV-specific antisera. The expressed protein had a size of approximately 108 kDA. The enzyme activity was not more sensitive to pyrophosphate analogues than the endogenous E.coli polymerases. Deletion of 51 nucleotides from the BALF5 DNA resulted in the removal of 17 amino acid residues from a portion of the potential 'leucine zipper' domain. Cells containing the deletion mutant failed to express a DNA polymerase activity which could be neutralized by EBV specific antisera.

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