TAILIEUCHUNG - Báo cáo khoa học: Insights into the Rrf2 repressor family – the structure of CymR, the global cysteine regulator of Bacillus subtilis

Pasteurella multocidatoxin (PMT) is a virulence factor responsible for the pathogenesis of somePasteurellosis. PMT exerts its toxic effects through the activation of heterotrimeric GTPase (Gq,G12⁄ 13 and Gi )-dependent pathways, by deamidating a glutamine residue in theasubunit of these GTPases. | IFEBS Journal Insights into the Rrf2 repressor family - the structure of CymR the global cysteine regulator of Bacillus subtilis William Shepard1 2 3 Olga Soutourina4 5 Emmanuelle Courtois4 5 Patrick England3 6 Ahmed Haouz2 3 and Isabelle Martin-Verstraete4 5 1 Synchrotron SOLEIL L Orme des Merisiers Saint Aubin BP48 Gif-sur-Yvette France 2 Institut Pasteur Plate-forme 6 Cristallogenese et Diffraction des Rayons X Paris France 3 CNRS-URA2185 Paris France 4 Institut Pasteur Laboratoire de Pathogenese des Bacteries Anaerobies Paris France 5 Universite Paris 7-Denis Diderot 75205 Paris France 6 Institut Pasteur Plate-forme de Biophysique des Macromolecules et de leurs Interactions Paris France Keywords crystal structure cysteine metabolism Fe-S clusters protein-DNA interaction Rrf2 repressor Correspondence I. Martin-Verstraete Laboratoire de Pathogenese des Bacteries Anaerobies Institut Pasteur 25 rue du Docteur Roux 75015 Paris France Fax 33 1 40 61 31 23 Tel 33 1 40 61 35 61 E-mail A. Haouz Plate-forme 6 Institut Pasteur 25 rue du Docteur Roux 75015 Paris France Fax 33 1 40 61 38 14 Tel 33 1 40 61 39 30 E-mail ahaouz@ The global regulator CymR represses the transcription of a large set of genes involved in cystine uptake and cysteine biosynthesis in Bacillus subtilis and Staphylococcus aureus. This repressor belongs to the widespread and poorly characterized Rrf2 family of regulators. The crystal structure of CymR from B. subtilis reveals a biologically active dimer where each monomer folds into two tightly packed domains a DNA-binding domain which houses a winged helix-turn-helix wHTH motif and a long dimerization domain which places the wHTH motifs at the extremes. This architecture explains how these small regulators can span 23-27-bp DNA targets. The wHTH motif of CymR resembles those of the GntR superfamily of regulators such as FadR and HutC. Superimposing the FadR wHTH motifs bound to their DNA fragments onto .

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