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An Autoinhibited State in the Structure of Thermotoga maritima NusG


Steiner,  Thomas
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Drögemueller, J., Stegmann, C. M., Mandal, A., Steiner, T., Burmann, B. M., Gottesman, M. E., et al. (2013). An Autoinhibited State in the Structure of Thermotoga maritima NusG. STRUCTURE, 21(3), 365-375. doi:10.1016/j.str.2012.12.015.

NusG is a conserved regulatory protein interacting with RNA polymerase (RNAP) and other proteins to form multicomponent complexes that modulate transcription. The crystal structure of Thermotoga maritima NusG (TmNusG) shows a three-domain architecture, comprising well-conserved amino-terminal (NTD) and carboxy-terminal (CTD) domains with an additional, species-specific domain inserted into the NTD. NTD and CTD directly contact each other, occluding a surface of the NTD for binding to RNAP and a surface on the CTD interacting either with transcription termination factor Rho or transcription antitermination factor NusE. NMR spectroscopy confirmed the intramolecular NTD-CTD interaction up to the optimal growth temperature of Thermotoga maritima. The domain interaction involves a dynamic equilibrium between open and closed states and contributes significantly to the overall fold stability of the protein. Wild-type TmNusG and deletion variants could not replace endogenous Escherichia coil NusG, suggesting that the NTD-CTD interaction of TmNusG represents an autoinhibited state.