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. 2013 Sep 23;41(Pt 5):1195–1200. doi: 10.1042/BST20130138

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© 2013 The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Licence (CC-BY)(http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

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(A) Structural model of the phosphorylation-induced conformational changes and oligomer assembly of NtrC (adapted with permission from [21,31]). The interfaces between the receiver domain and the AAA+ domain and that between the AAA+ domain and the HTH domain play important regulatory roles in various NtrC homologues through inter-domain allosteric control and determine transcription control stringency [32] (B) Engineering strategy for functional domain exchanged synthetic EBPs to rewire signalling networks. Engineered chimaeric EBPs are constructed by coupling the HTH DNA-binding domain of one EBP (e.g. NtrC) to the receiver and AAA+ domains of a non-cognate bEBPs such as ZraR (zinc), PspF (membrane stress), NorR (NO). The functional chimaera can then be selected out by interface-targeted mutagenesis by randomly mutating the linker region between the two coupled domains.