Chaperone OsmY facilitates the biogenesis of a major family of autotransporters
| Autor: | Zhen Yan, Xu Wang, Sunyia Hussain, Harris D. Bernstein, James C.A. Bardwell |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Protein Folding
Type V Secretion Systems Microbiology Article 03 medical and health sciences Protein Domains Escherichia coli Molecular Biology 030304 developmental biology Adhesins Escherichia coli 0303 health sciences biology 030306 microbiology Escherichia coli Proteins Gene Expression Regulation Bacterial Periplasmic space Cell biology Bacterial adhesin Proteostasis Periplasmic Binding Proteins Chaperone (protein) biology.protein Protein folding Bacterial outer membrane Biogenesis Molecular Chaperones Autotransporters |
| Zdroj: | Mol Microbiol |
| ISSN: | 1365-2958 0950-382X |
| DOI: | 10.1111/mmi.14358 |
| Popis: | OsmY is a widely conserved but poorly understood 20 kDa periplasmic protein. Using a folding biosensor, we previously obtained evidence that OsmY has molecular chaperone activity. To discover natural OsmY substrates, we screened for proteins that are destabilized and thus present at lower steady-state levels in an osmY-null strain. The abundance of an outer membrane protein called antigen 43 was substantially decreased and its β-barrel domain was undetectable in the outer membrane of an osmY-null strain. Antigen 43 is a member of the diffuse adherence family of autotransporters. Like strains that are defective in antigen 43 production, osmY-null mutants failed to undergo cellular autoaggregation. In vitro, OsmY assisted in the refolding of the antigen 43 β-barrel domain and protected it from added protease. Finally, an osmY-null strain that expressed two members of the diffuse adherence family of autotransporters that are distantly related to antigen 43, EhaA and TibA, contained reduced levels of the proteins and failed to undergo cellular autoaggregation. Taken together, our results indicate that OsmY is involved in the biogenesis of a major subset of autotransporters, a group of proteins that play key roles in bacterial pathogenesis. |
| Databáze: | OpenAIRE |
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