Structural and functional features of Crl proteins and identification of conserved surface residues required for interaction with the RpoS/σS subunit of RNA polymerase
| Autor: | Claudine Mayer, Frederick Saul, Ahmed Haouz, Patrick Weber, Véronique Monteil, Bertrand Raynal, Françoise Norel, Patrick England, Fabienne Levi-Acobas, Paola Cavaliere, Jacques Bellalou |
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| Přispěvatelé: | Génétique Moléculaire, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Production de Protéines Recombinantes (Plate-Forme) (PRPF), Cellule Pasteur, Université Paris Diderot - Paris 7 (UPD7)-PRES Sorbonne Paris Cité, Microbiologie structurale - Structural Microbiology (Microb. Struc. (UMR_3528 / U-Pasteur_5)), Institut Pasteur [Paris]-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Cristallographie (Plate-forme), Biophysique Moléculaire (Plate-forme), This work was supported by the French National Research Agency [grant number ANR-11-BSV3-009] and by the Institut Pasteur and the Centre National de la Recherche Scientifique., ANR-11-BSV3-0009,SIGMADAPT,Rôle de SigmaS dans la compétitivité et l'adaptation des bactéries à l'environnement(2011), Cristallographie (Plateforme) - Crystallography (Platform), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Salmonella typhimurium
Protein subunit Amino Acid Motifs Sigma Factor Plasma protein binding Biology Crystallography X-Ray MESH: Proteus mirabilis Biochemistry Conserved sequence 03 medical and health sciences chemistry.chemical_compound MESH: Amino Acid Motifs MESH: Protein Structure Tertiary Protein structure Bacterial Proteins Sigma factor RNA polymerase MESH: Protein Binding Binding site Molecular Biology Proteus mirabilis MESH: Bacterial Proteins Conserved Sequence 030304 developmental biology Genetics 0303 health sciences Binding Sites MESH: Conserved Sequence [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] 030302 biochemistry & molecular biology fungi food and beverages MESH: Sigma Factor MESH: Salmonella typhimurium [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Cell Biology DNA-Directed RNA Polymerases MESH: Crystallography X-Ray Cell biology Protein Structure Tertiary MESH: DNA-Directed RNA Polymerases [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] chemistry MESH: Binding Sites bacteria rpoS Protein Binding |
| Zdroj: | Biochemical Journal Biochemical Journal, Portland Press, 2014, 463 (2), pp.215-24. ⟨10.1042/BJ20140578⟩ Biochemical Journal, 2014, 463 (2), pp.215-24. ⟨10.1042/BJ20140578⟩ |
| ISSN: | 0264-6021 1470-8728 |
| DOI: | 10.1042/BJ20140578⟩ |
| Popis: | International audience; In many γ-proteobacteria, the RpoS/σS sigma factor associates with the core RNAP (RNA polymerase) to modify global gene transcription in stationary phase and under stress conditions. The small regulatory protein Crl stimulates the association of σS with the core RNAP in Escherichia coli and Salmonella enterica serovar Typhimurium, through direct and specific interaction with σS. The structural determinants of Crl involved in σS binding are unknown. In the present paper we report the X-ray crystal structure of the Proteus mirabilis Crl protein (CrlPM) and a structural model for Salmonella Typhimurium Crl (CrlSTM). Using a combination of in vivo and in vitro assays, we demonstrated that CrlSTM and CrlPM are structurally similar and perform the same biological function. In the Crl structure, a cavity enclosed by flexible arms contains two patches of conserved and exposed residues required for σS binding. Among these, charged residues that are likely to be involved in electrostatic interactions driving Crl-σS complex formation were identified. CrlSTM and CrlPM interact with domain 2 of σS with the same binding properties as with full-length σS. These results suggest that Crl family members share a common mechanism of σS binding in which the flexible arms of Crl might play a dynamic role. |
| Databáze: | OpenAIRE |
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