Characterization of theShigellaandSalmonellaType III Secretion System Tip-Translocon Protein-Protein Interaction by Paramagnetic Relaxation Enhancement
| Autor: | Roberto N. De Guzman, Srirupa Chatterjee, Kawaljit Kaur |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular 0301 basic medicine Salmonella Virulence Plasma protein binding medicine.disease_cause environment and public health Biochemistry Article Type three secretion system Protein–protein interaction 03 medical and health sciences Type III Secretion Systems medicine Shigella Nuclear Magnetic Resonance Biomolecular Molecular Biology 030102 biochemistry & molecular biology Chemistry Organic Chemistry Translocon 030104 developmental biology Ectodomain Biophysics Molecular Medicine lipids (amino acids peptides and proteins) Protein Binding |
| Zdroj: | ChemBioChem. 17:745-752 |
| ISSN: | 1439-4227 |
| DOI: | 10.1002/cbic.201500556 |
| Popis: | Many Gram-negative pathogens, such as Shigella and Salmonella, assemble the type III secretion system (T3SS) to inject virulence proteins directly into eukaryotic cells to initiate infectious diseases. The needle apparatus of the T3SS consists of a base, an extracellular needle, a tip protein complex, and a translocon. The atomic structure of the assembled tip complex and the translocon is unknown. Here, we show by NMR paramagnetic relaxation enhancement (PRE) that the mixed α-β domain at the distal region of the Shigella and Salmonella tip proteins interacts with the N-terminal ectodomain of their major translocon proteins. Our results reveal the binding surfaces involved in the tip-translocon protein-protein interaction and provide insights about the assembly of the needle apparatus of the T3SS. |
| Databáze: | OpenAIRE |
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