Biochemical characterization of the Yersinia YopT protease: Cleavage site and recognition elements in Rho GTPases

The Gram-negative bacterial pathogen Yersinia delivers six effector proteins into the host cells to thwart the host innate immune response. One of the effectors, YopT, causes the disruption of the actin cytoskeleton and contributes to the inhibition of phagocytosis of the pathogen. YopT functions as...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2003-02, Vol.100 (3), p.904-909
Hauptverfasser:	Shao, Feng, Vacratsis, Panayiotis O, Bao, Zhaoqin, Bowers, Katherine E, Fierke, Carol A, Dixon, Jack E
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - chemistry Bacterial Proteins - metabolism Biochemistry Biological Sciences cdc42 GTP-Binding Protein - metabolism Cell Line Chromatography, Thin Layer Cysteine - chemistry Cysteine Endopeptidases Cytotoxins Electrophoresis, Polyacrylamide Gel Glutathione Transferase - metabolism Glycine - chemistry Guanosine Diphosphate - metabolism Guanosine Triphosphate - metabolism Humans Lipid Metabolism Mass Spectrometry Neurotransmitters Plasmids - metabolism Protein Binding Protein Conformation Protein Prenylation Protein Structure, Tertiary Recombinant Proteins - metabolism rho GTP-Binding Proteins - metabolism rhoA GTP-Binding Protein - metabolism Transfection Yersinia pseudotuberculosis - enzymology
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