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- W1520771983 abstract "The O6-alkylguanine DNA alkyltransferase (AGT) is a DNA repair enzyme that binds DNA with moderate cooperativity. This cooperativity is important for its search for alkylated bases. A structural model of the cooperative complex of AGT with DNA predicts short-range interactions between nearest protein neighbors and long-range interactions between proteins separated in the array. DNA substrates ranging from 11bp to 30bp allowed us to use differences in binding stoichiometry to resolve short- and long-range protein contributions to the stability of AGT complexes. We found that the short-range component of ΔG°coop was nearly independent of DNA length and protein packing density. In contrast the long-range component oscillated with DNA length, with a period equal to the occluded binding site size (4bp). The amplitude of the long-range component decayed from ∼−4 kcal/mole of interaction to ∼−1.2 kcal/mol of interaction as the size of cooperative unit increased from 4 to 7 proteins, suggesting a mechanism to limit the size of cooperative clusters. These features allow us to make testable predictions about AGT distributions and interactions with chromatin structures in vivo. © 2015 The Authors Biopolymers Published by Wiley Periodicals, Inc. Biopolymers 103: 509–516, 2015." @default.
- W1520771983 created "2016-06-24" @default.
- W1520771983 creator A5007320411 @default.
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- W1520771983 date "2015-06-26" @default.
- W1520771983 modified "2023-09-26" @default.
- W1520771983 title "Resolving the contributions of two cooperative mechanisms to the<scp>DNA</scp>Binding of<scp>AGT</scp>" @default.
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- W1520771983 doi "https://doi.org/10.1002/bip.22684" @default.
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