Characterization of 3'-to 5'-exonuclease activity associated with Epstein-Barr virus DNA polymerase.

Abstract:

:Epstein-Barr virus (EBV) DNA polymerase mediates viral DNA replication during the lytic phase of the EB virus life cycle. In order to characterize its enzymatic activities EBV DNA polymerase was purified more than 1200-fold from chemically induced B95-8 cells. One polypeptide with molecular weight of 110,000 corresponded to the predicted EBV DNA polymerase, whereas the other polypeptides did not. A 3'-to-5' exonuclease activity was copurified with the EBV DNA polymerase through the course of the purification. Unlike HSV DNA DNA polymerase, 5'-to-3' exonuclease activity was not associated with the EBV DNA polymerase on the final step chromatography of single-stranded DNA agarose column. The associated 3'-to-5' exonuclease activity was stimulated by ammonium sulfate like the polymerase activity. It exhibited DNA-dependent nucleotide turnover activity and preferentially excised a terminal mismatched nucleotide on hybridized polynucleotides compared to the correctly paired substrate, indicating that the 3'-to-5' exonuclease may play a role in proofreading in the polymerization process.

journal_name

Virology

journal_title

Virology

authors

Tsurumi T

doi

10.1016/0042-6822(91)90685-5

subject

Has Abstract

pub_date

1991-05-01 00:00:00

pages

376-81

issue

1

eissn

0042-6822

issn

1096-0341

pii

0042-6822(91)90685-5

journal_volume

182

pub_type

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