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ability to follow the polarization of the molecule as it negotiates DNA; this is an
important measure of whether or not the molecule follows the helical pitch of
the DNA.
Recent technical advances have allowed for the development of new single-
molecule approaches to study how proteins interact with DNA. A physical
description of these interactions is vital as simply knowing the sequence of events
only describes half of the picture. Furthermore, bulk methods average behavior
across the entire population, whereas single-molecule approaches allow for a
complete description of the various heterogeneous pathways and processes that
molecules undertake in reality. This is clearly evident from the number of modes
of motion that UvrAB employs to find its target site. The next challenge that faces
the field is to construct more complex systems, and watch the entire process of
NER occur in real time. First, this will be achieved in vitro and, ultimately,
in vivo. 39 Though this is not an easy challenge, as our approaches become more
interdisciplinary, it is both a worthy and attainable one.
References
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Chemical carcinogenesis, current cancer research . New York, NY: Springer Science
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Business Media, LLC; 2011.
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excision repair protein in complex with modified DNA. Nat Struct Mol Biol 2011;
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3. Croteau DL, DellaVecchia MJ, Perera L, Van Houten B. Cooperative damage recognition by
UvrA and UvrB: identification of UvrA residues that mediate DNA binding. DNA Repair
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C-terminal zinc finger of UvrA does not bind DNA directly but regulates damage-specific
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7. Van Houten B, Gamper H, Hearst JE, Sancar A. Analysis of sequential steps of nucleotide
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adducts. J Biol Chem 1988;
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8. Truglio JJ, Croteau DL, Van Houten B, Kisker C. Prokaryotic nucleotide excision repair: the
UvrABC system. Chem Rev 2006;
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9. Van Houten B, Croteau DL, DellaVecchia MJ, Wang H, Kisker C. ''Close-fitting sleeves'':
DNA damage recognition by the UvrABC nuclease system. Mutat Res 2005;
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basis for DNA recognition and processing by UvrB. Nat Struct Mol Biol 2006;
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