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• W2035520565 abstract "Replication protein A (RPA) plays an essential role in DNA replication by binding and unfolding non-canonical single-stranded DNA (ssDNA) structures. Of the six RPA ssDNA binding domains (labeled A-F), RPA-CDE selectively binds a G-quadruplex forming sequence (<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msup><mml:mn>5</mml:mn><mml:mo>′</mml:mo></mml:msup></mml:math>-TAGGGGAAGGGTTGGAGTGGGTT-<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msup><mml:mn>3</mml:mn><mml:mo>′</mml:mo></mml:msup></mml:math>called Gq23). In K + , Gq23 forms a mixed parallel/antiparallel conformation, and in Na + Gq23 has a less stable (<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mrow><mml:msub><mml:mi>T</mml:mi><mml:mi>M</mml:mi></mml:msub></mml:mrow></mml:math>lowered by ∼<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msup><mml:mi>20</mml:mi><mml:mn>∘</mml:mn></mml:msup></mml:math>C), antiparallel conformation. Gq23 is intramolecular and 1D NMR confirms a stable G-quadruplex structure in K + . Full-length RPA and RPA-CDE-core can bind and unfold the Na + form of Gq23 very efficiently, but complete unfolding is not observed with the K + form. Studies with G-quadruplex ligands, indicate that TMPyP4 has a thermal stabilization effect on Gq23 in K + , and inhibits complete unfolding by RPA and RPA-CDE-core. Overall these data indicate that G-quadruplexes present a unique problem for RPA to unfold and ligands, such as TMPyP4, could possibly hinder DNA replication by blocking unfolding by RPA." @default.
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• W2035520565 date "2011-01-01" @default.
• W2035520565 modified "2023-10-17" @default.
• W2035520565 title "Stabilization of a G-Quadruplex from Unfolding by Replication Protein A Using Potassium and the Porphyrin TMPyP4" @default.
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• W2035520565 doi "https://doi.org/10.4061/2011/529828" @default.
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