Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion

Many bacterial pathogens use a type III protein secretion system to deliver virulence effector proteins directly into the host cell cytosol, where they modulate cellular processes. A requirement for the effective translocation of several such effector proteins is the binding of specific cytosolic ch...

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Veröffentlicht in:	Nature (London) 2001-11, Vol.414 (6859), p.77-81
Hauptverfasser:	Galán, Jorge E, Stebbins, C. Erec
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacteria Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacterial Proteins - secretion Bacteriology Biological and medical sciences Chaperonins - metabolism Crystallography, X-Ray Fundamental and applied biological sciences. Psychology GTPase-Activating Proteins - chemistry GTPase-Activating Proteins - metabolism Humanities and Social Sciences letter Microbiology Models, Molecular Molecular biology Molecules multidisciplinary Pathogens Peptides Permeability, membrane transport, intracellular transport Protein Binding Protein Conformation Protein Folding Protein Tyrosine Phosphatases - chemistry Protein Tyrosine Phosphatases - metabolism Protein Tyrosine Phosphatases - secretion Proteins Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Salmonella Salmonella typhimurium - metabolism Salmonella typhimurium - pathogenicity Science Science (multidisciplinary) SicP protein SptP protein Translocation Virulence
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