The crystal structure of the anti-σ factor CnrY in complex with the σ factor CnrH shows a new structural class of anti-σ factors targeting extracytoplasmic function σ factors.

Abstract : Gene expression in bacteria is regulated at the level of transcription initiation, a process driven by σ factors. The regulation of σ factor activity proceeds from the regulation of their cytoplasmic availability, which relies on specific inhibitory proteins called anti-σ factors. With anti-σ factors regulating their availability according to diverse cues, extracytoplasmic function σ factors (σ(ECF)) form a major signal transduction system in bacteria. Here, structure:function relationships have been characterized in an emerging class of minimal-size transmembrane anti-σ factors, using CnrY from Cupriavidus metallidurans CH34 as a model. This study reports the 1.75-Å-resolution structure of CnrY cytosolic domain in complex with CnrH, its cognate σ(ECF), and identifies a small hydrophobic knob in CnrY as the major determinant of this interaction in vivo. Unsuspected structural similarity with the molecular switch regulating the general stress response in α-proteobacteria unravels a new class of anti-σ factors targeting σ(ECF). Members of this class carry out their function via a 30-residue stretch that displays helical propensity but no canonical structure on its own.
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Article dans une revue
Journal of Molecular Biology, Elsevier, 2014, 426 (12), pp.2313-27
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http://hal.univ-grenoble-alpes.fr/hal-01119790
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Soumis le : mardi 24 février 2015 - 09:45:36
Dernière modification le : jeudi 11 janvier 2018 - 06:22:39

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  • HAL Id : hal-01119790, version 1
  • PUBMED : 24727125

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Antoine P Maillard, Eric Girard, Widade Ziani, Isabelle Petit-Härtlein, Richard Kahn, et al.. The crystal structure of the anti-σ factor CnrY in complex with the σ factor CnrH shows a new structural class of anti-σ factors targeting extracytoplasmic function σ factors.. Journal of Molecular Biology, Elsevier, 2014, 426 (12), pp.2313-27. 〈hal-01119790〉

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