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ATPase-Independent Type-III Protein Secretion in


The type-III protein secretion apparatus is a complex nanomachine responsible for secretion of building blocks and substrate proteins of the flagellum and the virulence-associated injectisome needle complex of many gram-negative pathogens. Type-III secretion systems utilize the energy of the proton motive force and ATP hydrolysis of a cytoplasmic ATPase to drive substrate export. The cytoplasmic components of the secretion system share strong homology to the FoF1 ATP synthase and it is thought that the flagellum was derived from a proto FoF1-ATP synthase where ATP hydrolysis energized the export process. Here, we report the dispensability of ATPase activity for the type-III protein export process in Salmonella. This finding has important implications for the evolution of the bacterial flagellum and type-III secretion systems, suggesting that a proto ATPase was added to a primordial proton-powered type-III export system with the evolutionary benefit of facilitating the export process.


Vyšlo v časopise: ATPase-Independent Type-III Protein Secretion in. PLoS Genet 10(11): e32767. doi:10.1371/journal.pgen.1004800
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1004800

Souhrn

The type-III protein secretion apparatus is a complex nanomachine responsible for secretion of building blocks and substrate proteins of the flagellum and the virulence-associated injectisome needle complex of many gram-negative pathogens. Type-III secretion systems utilize the energy of the proton motive force and ATP hydrolysis of a cytoplasmic ATPase to drive substrate export. The cytoplasmic components of the secretion system share strong homology to the FoF1 ATP synthase and it is thought that the flagellum was derived from a proto FoF1-ATP synthase where ATP hydrolysis energized the export process. Here, we report the dispensability of ATPase activity for the type-III protein export process in Salmonella. This finding has important implications for the evolution of the bacterial flagellum and type-III secretion systems, suggesting that a proto ATPase was added to a primordial proton-powered type-III export system with the evolutionary benefit of facilitating the export process.


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