The role of EscD in supporting EscC polymerization in the type III secretion system of enteropathogenic Escherichia coli
| Autor: | Sonia Oren, Avner Dagan, Irit Tseytin, Neta Sal-Man |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Immunoblotting Biophysics Virulence Plasma protein binding Biology Biochemistry Type three secretion system Polymerization 03 medical and health sciences Enteropathogenic Escherichia coli Type III Secretion Systems Protein oligomerization Amino Acid Sequence Peptide sequence Binding Sites Escherichia coli Proteins Cell Membrane Membrane Proteins Cell Biology Transmembrane domain 030104 developmental biology Membrane protein Protein Multimerization Protein Binding |
| Zdroj: | Biochimica et biophysica acta. Biomembranes. 1860(2) |
| ISSN: | 0005-2736 |
| Popis: | The type III secretion system (T3SS) is a multi-protein complex that plays a central role in the virulence of many Gram-negative bacterial pathogens. In enteropathogenic Escherichia coli, a prevalent cause of diarrheal diseases, the needle complex base of the T3SS is formed by multi-rings: two concentric inner-membrane rings made by the two oligomerizing proteins (EscD and EscJ), and an outer ring made of a single oligomerizing protein (EscC). Although the oligomerization activity of these proteins is critical for their function and can, therefore, affect the virulence of the pathogen, the mechanisms underlying the oligomerization of these proteins have yet to be identified. In this study, we report that the proteins forming the inner-membrane T3SS rings, EscJ and EscD proteins, are crucial for the oligomerization of EscC. Moreover, we elucidate the oligomerization process of EscD and determine the contribution of individual regions of the protein to its self-oligomerization activity. We show that the oligomerization motif of EscD is located at its N-terminal portion and that its transmembrane domain can self-oligomerize, thus contributing to the self-oligomerization of the full-length EscD. |
| Databáze: | OpenAIRE |
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