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

Autor: Eric Girard, Antoine P. Maillard, Jacques Covès, Isabelle Petit-Härtlein, Richard Kahn, Widade Ziani
Přispěvatelé: CHU Pontchaillou [Rennes], Thales Alenia Space (TAS), THALES, Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Bureau d'Économie Théorique et Appliquée (BETA), Institut National de la Recherche Agronomique (INRA)-Université de Strasbourg (UNISTRA)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Department of Psychiatry, University Medical Center [Utrecht]-Brain Center Rudolf Magnus, Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2014
Předmět:
Models
Molecular
Protein Conformation
Structural similarity
Sigma Factor
Plasma protein binding
Crystallography
X-Ray
Protein–protein interaction
MESH: Protein Conformation
Protein structure
Structural Biology
Sigma factor
Bacterial transcription
MESH: Protein Binding
Protein Interaction Domains and Motifs
Molecular Biology
MESH: Cupriavidus
MESH: Protein Interaction Domains and Motifs
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
biology
Cupriavidus metallidurans
Cupriavidus
MESH: Sigma Factor
MESH: Crystallography
X-Ray
biology.organism_classification
Transmembrane protein
Repressor Proteins
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
Crystallography
MESH: Repressor Proteins
Biophysics
MESH: Models
Molecular
Protein Binding
Zdroj: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2014, 426 (12), pp.2313-27
ISSN: 0022-2836
1089-8638
DOI: 10.1016/j.jmb.2014.04.003
Popis: International audience; 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.
Databáze: OpenAIRE
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