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J Biol Chem, Vol. 274, Issue 30, 20749-20752, July 23, 1999
Depends on
Interactions in the DNA Minor Groove
,§
From the To examine the hypothesis that interactions
between a DNA polymerase and the DNA minor groove are critical for
accurate DNA synthesis, we studied the fidelity of DNA polymerase Laboratory of Molecular Genetics and
§ Laboratory of Structural Biology, NIEHS, Research Triangle
Park, North Carolina 27709
mutants at residue Arg283, where arginine, which
interacts with the minor groove at the active site, is replaced by
alanine or lysine. Alanine substitution, removing minor groove
interactions, strongly reduces polymerase selectivity for all
single-base mispairs examined. In contrast, the lysine substitution,
which retains significant interactions with the minor groove, has
wild-type-like selectivity for T·dGMP and A·dGMP mispairs but
reduced selectivity for T·dCMP and A·dCMP mispairs. Examination of
DNA crystal structures of these four mispairs indicates that the two
mispairs excluded by the lysine mutant have an atom (N2) in an
unfavorable position in the minor groove, while the two mispairs
permitted by the lysine mutant do not. These results suggest that
unfavorable interactions between an active site amino acid side chain
and mispair-specific atoms in the minor groove contribute to DNA
polymerase specificity.
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