Model and assay for dsDNA binding by RdgC dimer

Copyright information:Taken from "The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding"Nucleic Acids Research 2007;35(8):2671-2681.Published online 10 Apr 2007PMCID:PMC1885664.© 2007 The Author(s) () Electrostatic potential at the molecular surface...

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Hauptverfasser: Ha, Jun Yong, Kim, Hye Kyong, Kim, Do Jin, Kim, Kyoung Hoon, Oh, Sung Jin, Lee, Hyung Ho, Yoon, Hye Jin, Song, Hyun Kyu, Suh, Se Won
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Zusammenfassung:Copyright information:Taken from "The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding"Nucleic Acids Research 2007;35(8):2671-2681.Published online 10 Apr 2007PMCID:PMC1885664.© 2007 The Author(s) () Electrostatic potential at the molecular surface of RdgC dimer. The molecular surface was colored according to the electrostatic potential (positive in blue and negative in red). () A proposed model of the complex between RdgC dimer and dsDNA (22-mer). () Residues that are suggested to interact with dsDNA by the complex model. Residues selected for mutagenesis are colored in blue. DNA is shown in sticks. () Electrophoretic mobility shift assay for dsDNA binding by RdgC. Detailed reaction conditions are described in the Materials and methods section. Lane 1, 200 bp dsDNA ladder marker; lane 2, dsDNA (414 bp); lane 3, wild type; lane 4, R4A mutant; lane 5, K70D mutant; lane 6, R81D mutant; lane 7, R122D mutant; lane 8, K146A mutant; lane 9, R198A mutant; lane 10, R208A mutant; lane 11, R211D mutant; lane 12, R252A mutant; lane 13, F120A mutant; lane 14, Q212A mutant; lane 15, dsDNA (414 bp).
DOI:10.6084/m9.figshare.16787