The YscE/YscG chaperone and YscF N-terminal sequences target YscF to the Yersinia pestis type III secretion apparatus
| Autor: | Michael Schwartz, YoSon Park, Julie Torruellas Garcia, Gregory V. Plano, Kristian L. Richards, Sara Schesser Bartra, Clarice de Azevedo Souza |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Cytoplasm Yersinia pestis Two-hybrid screening Protein subunit 030106 microbiology Gene Expression Protein Sorting Signals Microbiology DNA-binding protein 03 medical and health sciences Bacterial Proteins Mutant protein Type III Secretion Systems Secretion biology Chemistry Membrane Proteins Gene Expression Regulation Bacterial biology.organism_classification Cell biology 030104 developmental biology Secretory protein Chaperone (protein) Mutation biology.protein Protein Multimerization Molecular Chaperones Protein Binding Research Article |
| Zdroj: | Microbiology. 164:338-348 |
| ISSN: | 1465-2080 1350-0872 |
| DOI: | 10.1099/mic.0.000610 |
| Popis: | The needle structures of type III secretion (T3S) systems are formed by the secretion and polymerization of a needle subunit protein, YscF in Yersinia pestis. A subset of T3S systems employ unique heterodimeric chaperones, YscE and YscG in Y. pestis, to prevent the polymerization of needle subunits within the bacterial cell. We demonstrate that the YscE/YscG chaperone is also required for stable YscF expression and for secretion of YscF. Overexpression of a functional maltose-binding protein (MBP)–YscG hybrid protein stabilized cytoplasmic YscF but YscF was not secreted in the absence of YscE. Furthermore, a YscE mutant protein was identified that functioned with YscG to stabilize cytosolic YscF; however, YscF was not secreted. These findings confirm a role for the YscE/YscG chaperone in YscF secretion and suggest that YscE may have a specific role in this process. Recent studies have shown that YscF deleted of its N-terminal 15 residues is still secreted and functional, suggesting that YscF may not require an N-terminal secretion signal. However, we demonstrate that YscF contains an N-terminal secretion signal and that a functional N-terminal signal is required for YscF secretion. |
| Databáze: | OpenAIRE |
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