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Vol. 15, No. 8, pp. 945-954, April 15, 2001
and 
and of Rev1 in the bypass of abasic sites
1 Sealy Center for Molecular Science, University of Texas
Medical Branch, Galveston, Texas 77555-1061, USA; 2 Department
of Biochemistry and Molecular Biophysics, Washington University School
of Medicine, St. Louis, Missouri 63110, USA
Abasic (AP) sites are one of the most frequently formed lesions in
DNA, and they present a strong block to continued synthesis by the
replicative DNA machinery. Here we show efficient bypass of an AP site
by the combined action of yeast DNA polymerases 
and 
. In this
reaction, Pol inserts an A nucleotide opposite the AP site, and
Pol subsequently extends from the inserted nucleotide. Consistent
with these observations, sequence analyses of mutations in the yeast
CAN1s gene indicate that A is the nucleotide inserted
most often opposite AP sites. The nucleotides C, G, and T are also
incorporated, but much less frequently. Enzymes such as Rev1 and Pol
may contribute to the insertion of these other nucleotides; the
predominant role of Rev1 in AP bypass, however, is likely to be
structural. Steady-state kinetic analyses show that Pol is highly
inefficient in incorporating nucleotides opposite the AP site, but it
efficiently extends from nucleotides, particularly an A, inserted
opposite this lesion. Thus, in eukaryotes, bypass of an AP site
requires the sequential action of two DNA polymerases, wherein the
extension step depends solely upon Pol, but the insertion step can
be quite varied, involving not only the predominant action of the
replicative DNA polymerase, Pol, but also the less prominent role of
various translesion synthesis polymerases.
[Key Words:
Abasic sites; mutagenic bypass; yeast; DNA
polymerase ; DNA polymerase ]
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