TAILIEUCHUNG - Báo cáo khoa học: Type III secretion system translocator has a molten globule conformation both in its free and chaperone-bound forms

Type III secretion systems of Gram-negative pathogenic bacteria allow the injection of effector proteins into the cytosol of host eukaryotic cells. Cros-sing of the eukaryotic plasma membrane is facilitated by a translocon, an oligomeric structure made up of two bacterial proteins inserted into the host membrane during infection. | ỊFEBS Journal Type III secretion system translocator has a molten globule conformation both in its free and chaperone-bound forms Eric Faudry1 Viviana Job2 Andrea Dessen2 Ina Attree1 and Vincent Forge3 1 CEA Grenoble DSV-iRTSV Laboratoire de Biochimie et Biophysique des Systemes Integres UMR5092 CNRS CEA Universite Joseph Fourier Grenoble France 2 Institut de Biologie Structurale Jean-Pierre Ebel UMR5075 CNRS CEA Universite Joseph Fourier Grenoble France 3 CEA Grenoble DSV-iRTSV Laboratoire de Chimie et Biologie des Metaux UMR5249 CNRS CEA Universite Joseph Fourier Grenoble France Keywords chaperones molten globule pore-forming toxins translocator type III secretion system Correspondence V. Forge CEA Grenoble DSV-iRTSV Laboratoire de Chimie et Biologie des Metaux UMR 5249 17 rue des martyrs 38054 Grenoble Cedex 9 France Fax 33 4 38 78 54 87 Tel 33 4 38 78 94 05 E-mail These authors contributed equally to this work Received 22 March 2007 revised 11 May 2007 accepted 17 May 2007 doi Type III secretion systems of Gram-negative pathogenic bacteria allow the injection of effector proteins into the cytosol of host eukaryotic cells. Crossing of the eukaryotic plasma membrane is facilitated by a translocon an oligomeric structure made up of two bacterial proteins inserted into the host membrane during infection. In Pseudomonas aeruginosa a major human opportunistic pathogen these proteins are PopB and PopD. Their interactions with their common chaperone PcrH in the cytosol of the bacteria are essential for the proper function of the injection system. The interaction region between PopD and PcrH was identified using limited proteolysis revealing that the putative PopD transmembrane fragment is buried within the PopD PcrH complex. In addition structural features of PopD and PcrH either individually or within the binary complex were characterized using spectroscopic methods and 1D NMR. Whereas PcrH possesses the .

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