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J Biol Chem, Vol. 274, Issue 45, 31763-31766, November 5, 1999
From the Department of Biological Chemistry, Weizmann Institute of
Science, Rehovot 76100, Israel
Replication of DNA lesions leads to the formation
of mutations. In Escherichia coli this process is regulated
by the SOS stress response, and requires the mutagenesis proteins UmuC
and UmuD'. Analysis of translesion replication using a recently
reconstituted in vitro system (Reuven, N. B., Tomer,
G., and Livneh, Z. (1998) Mol. Cell 2, 191-199) revealed
that lesion bypass occurred with a UmuC fusion protein, UmuD', RecA,
and SSB in the absence of added DNA polymerase. Further analysis
revealed that UmuC was a DNA polymerase (E. coli DNA
polymerase V), with a weak polymerizing activity. Upon addition of
UmuD', RecA, and SSB, the UmuC DNA polymerase was greatly activated,
and replicated a synthetic abasic site with great efficiency (45%
bypass in 6 min), 10-100-fold higher than E. coli DNA
polymerases I, II, or III holoenzyme. Analysis of bypass products
revealed insertion of primarily dAMP (69%), and to a lesser degree
dGMP (31%) opposite the abasic site. The UmuC104 mutant protein was
defective both in lesion bypass and in DNA synthesis. These results
indicate that UmuC is a UmuD'-, RecA-, and SSB-activated DNA
polymerase, which is specialized for lesion bypass. UmuC is a member of
a new family of DNA polymerases which are specialized for lesion
bypass, and include the yeast RAD30 and the human
XP-V genes, encoding DNA polymerase 
.
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