Hook‐basal‐body assembly state dictates substrate specificity of the flagellar type‐III secretion system
| Autor: | Manuel Halte, Marc Erhardt, Svenja Hüsing, Alina Guse |
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| Jazyk: | angličtina |
| Předmět: |
Motility
570 Biologie Flagellum Biology Microbiology Substrate Specificity Type three secretion system 03 medical and health sciences Bacterial Proteins ddc:570 Type III Secretion Systems Basal body Secretion Molecular Biology 030304 developmental biology substrate specificity switching 0303 health sciences 030306 microbiology Membrane Proteins Salmonella enterica Substrate (chemistry) Basal Bodies Transport protein Cell biology Crosstalk (biology) motility type‐III secretion Flagella flagella biosynthesis protein transport |
| Zdroj: | Molecular Microbiology. 116(4):1189-1200 |
| ISSN: | 1365-2958 0950-382X |
| DOI: | 10.1111/mmi.14805 |
| Popis: | The assembly of the bacterial flagellum is orchestrated by the secretion of distinct early and late secretion substrates via the flagellar‐specific type‐III secretion system (fT3SS). However, how the fT3SS is able to distinguish between the different (early and late) substrate classes during flagellar assembly remains poorly understood. In this study, we investigated the substrate selectivity and specificity of the fT3SS of Salmonella enterica at different assembly stages. For this, we developed an experimental setup that allowed us to synchronize hook‐basal‐body assembly and to monitor early and late substrate secretion of fT3SSs operating in either early or late secretion mode, respectively. Our results demonstrate that the fT3SS features a remarkable specificity for only the substrates required at the respective assembly stage. No crosstalk of substrates was observed for fT3SSs operating in the opposing secretion mode. We further found that a substantial fraction of fT3SS surprisingly remained in early secretion mode. Our results thus suggest that the secretion substrate specificity switch of the fT3SS is unidirectional and irreversible. The developed secretion substrate reporter system further provides a platform for future investigations of the underlying molecular mechanisms of the elusive substrate recognition of the T3SS. H2020 European Research Council http://dx.doi.org/10.13039/100010663 Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659 Humboldt‐Universität zu Berlin http://dx.doi.org/10.13039/501100006211 |
| Databáze: | OpenAIRE |
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