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Figure 1.
Fig. 1. A, multiple amino acid alignment of the 8-kDa
domain of human Pol  with the
other human family X DNA polymerases. Residues described to be
relevant to the 8-kDa domain function of Pol  (His34,
Lys35, Tyr39, Lys60, Lys68, Glu71, Lys72, Glu75, and Lys84) are
indicated in white letters over a black background. The position
of Lys310 (Pol residue
Lys72) is indicated with an asterisk. Invariant (bold type) and
conservative substitutions referred to Pol residues
are boxed in dark and light gray, respectively. The arrow
indicates the position of proteolytic cleavage for Pol . B,
schematic representation of a dRP lyase reaction. A 34-mer
double-stranded oligonucleotide containing an uracil residue at
position 16 in one strand is treated with hUDG and hAPE to
release a dRP-containing substrate. This dRP moiety will be
cleaved by dRP lyase activity. C, autoradiogram illustrating Pol
dRP lyase
activity. 10-Min reactions were performed as described under
"Experimental Procedures," using 50 nM Pol , 80 nM
(wild-type) or 100 nM (K310A mutant) Pol . Asterisk
indicates the use of a reduced AP substrate.
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