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|Title:||A Divalent Metal-mediated Switch Controlling Protein-induced DNA Bending||Authors:||Bao, Q.
DNA architectural proteins
integration host factor
nucleoprotein complex formation
|Issue Date:||30-Mar-2007||Citation:||Bao, Q., Chen, H., Liu, Y., Yan, J., Dröge, P., Davey, C.A. (2007-03-30). A Divalent Metal-mediated Switch Controlling Protein-induced DNA Bending. Journal of Molecular Biology 367 (3) : 731-740. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jmb.2006.09.082||Abstract:||Architectural proteins that reconfigure the paths of DNA segments are required for the establishment of functional interfaces in many genomic transactions. A single-chain derivative of the DNA architectural protein integration host factor was found to adopt two stable conformational states in complex with a specific DNA target. In the so-called open state, the degree of protein-induced DNA bending is reduced significantly compared with the closed state. The conformational switch between these states is controlled by divalent metal binding in two electronegative zones arising from the lysine-to-glutamate substitution in the protein body proximal to the phosphate backbone of one DNA arm. We show that this switch can be employed to control the efficiency of site-specific recombination catalyzed by λ integrase. Introduction of acidic residues at the protein-DNA interface holds potential for the design of metal-mediated switches for the investigation of functional relationships. © 2006 Elsevier Ltd. All rights reserved.||Source Title:||Journal of Molecular Biology||URI:||http://scholarbank.nus.edu.sg/handle/10635/95617||ISSN:||00222836||DOI:||10.1016/j.jmb.2006.09.082|
|Appears in Collections:||Staff Publications|
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