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J. Biol. Chem., Vol. 277, Issue 41, 38339-38344, October 11, 2002
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From the Department of Chemistry, Temple University,
Philadelphia, Pennsylvania 19122
DNA Photolyase is a flavoprotein that uses light
to repair cyclobutylpyrimidine dimers in DNA. From considerations of
the crystal structure of the protein, it has been hypothesized that the
dimer lesion is flipped out of the DNA double helix into the substrate
binding pocket. We have used a fluorescent adenine analog, 2-aminopurine (2-Ap), as a probe of local double helical structure upon
binding of the substrate to the protein. Our results show that the
local structure around the thymidine lesion changes dramatically upon
binding to Photolyase. This is consistent with base flipping of the
lesion into the protein binding cavity with concomitant destacking of
the opposing complementary 2-Ap nucleotide.
Cyclobutylpyrimidine Dimer Base Flipping by DNA
Photolyase*
,
*
This work was supported by Grant MCB 9982532 from the
National Science Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by an Undergraduate Biological Science Education Program
Grant from the Howard Hughes Medical Institute. Present address: Dept.
of Medicine and Center for Human Genetics, Duke University Medical
Center, Durham, NC 27710.
§
To whom correspondence should be addressed: Dept. of Chemistry,
Temple University, 201 Beury Hall, Philadelphia, PA 19122. Tel.:
215-204-2027; Fax: 215-204-1532; E-mail:
robert.stanley@temple.edu.
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