Nucleic Acids Research, Vol 25, Issue 9 1745-1752, Copyright © 1997 by Oxford University Press
AJ King, WR Teertstra, L Blanco, M Salas and PC van der Vliet
By using a baculovirus expression system, the adenovirus (Ad) DNA
polymerase was purified to homogeneity and shown to display a 3'--
>5'exonuclease activity which is coupled to the polymerase activity. On
a partial duplex structure the exonuclease activity had a marked preference
for excision of a mismatched versus a matched 3'-terminus, which enables
the Ad DNA polymerase to act as a proofreading enzyme. On single-stranded
DNA the exonuclease action is distributive, but during replication removal
of mismatched nucleotides and the switch to synthesis occurs without
dissociation of the polymerase from the template. When the Ad DNA
polymerase is bound to the precursor terminal protein, the rate of
exonucleolysis was four times slower. Moreover, degradation could not
proceed as far as with the free Ad polymerase, indicating also a
qualitative difference. These results suggest a reduced proofreading
capacity of the precursor terminal protein- polymerase complex, which might
affect the initial stages of DNA replication.
ARTICLES
Processive proofreading by the adenovirus DNA polymerase. Association with the priming protein reduces exonucleolytic degradation
Laboratory for Physiological Chemistry, University of Utrecht, PO Box 80042, 3508 TA Utrecht, The Netherlands.
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