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Wild-type DNA polymerase II (pol II) and an
exonuclease-deficient pol II mutant (D155A/E157A) have been
overexpressed and purified in high yield from Escherichia
coli. Wild-type pol II exhibits a high proofreading 3`-exonuclease
to polymerase ratio, similar in magnitude to that observed for
bacteriophage T4 DNA polymerase. While copying a 250-nucleotide region
of the lacZ
Volume 270,
Number 25,
Issue of June 23, pp. 15327-15335, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
gene, the fidelity of wild-type pol II is
high, with error rates for single-base substitution and frameshift
errors being 
10. In contrast, the pol II
exonuclease-deficient mutant generated a variety of base substitution
and single base frameshift errors, as well as deletions between both
perfect and imperfect directly repeated sequences separated by a few to
hundreds of nucleotides. Error rates for the pol II
exonuclease-deficient mutant were from
13- to 240-fold higher
than for wild-type pol II, depending on the type of error considered.
These data suggest that from 90 to >99% of base substitutions,
frameshifts, and large deletions are efficiently proofread by the
enzyme. The results of these experiments together with recent in
vivo studies suggest an important role for pol II in the fidelity
of DNA synthesis in cells.
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