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Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity

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Toxin-antitoxin (TA) modules are small stress response operons encoding a toxin that targets transcription and/or translation and a corresponding neutralizing antitoxin. They are involved in the stabilization of low copy number plasmids and may play a role in the stress physiology of bacteria. While the relevance and cellular actions of TA modules are becoming clear, the regulation at the molecular level remains a challenging topic. The regulation of toxin-antitoxin operons usually involves the toxin acting as co- or de-repressor depending on the ratio toxin/antitoxin. This unexplained transcriptional regulatory phenomenon is known as conditional cooperativity. Using the phd/doc operon as model system, we have found that binding of the toxin Doc to the C-terminal intrinsically disordered segment of Phd, induces order in the N-terminal DNA binding domain of Phd(1). Based on substantial structural and biophysical evidences we propose a model for the conditional cooperative regulation of transcription, typical of TA systems, that involves allosteric coupling between two partially disordered domains, which may be applicable for the regulation of other biological systems.

(1) Garcia-Pino A., Balasubramanian S., L., Ehud Gazit E., Magnuson R.D., Charlier D., Loris R., Transcriptional regulation by conditional co-operativity mediated by allosteric coupling between two disordered domains. (2010) Cell Jul 9;142(1):101-11

(2) De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. Mol Cell. (2009) Jul 31;35(2):154-6

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