The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion
Protein secretion through type-three secretion systems (T3SS) is critical for motility and virulence of many bacteria. Proteins are transported through an export gate containing three proteins (FliPQR in flagella, SctRST in virulence systems). A fourth essential T3SS protein (FlhB/SctU) functions to...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Nature Research
2020
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| _version_ | 1797074912292110336 |
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| author | Kuhlen, L Johnson, S Andreas Zeitler Baurle, S Deme, J Caesar, J Debo, R Fisher, J Wagner, S Lea, S |
| author_facet | Kuhlen, L Johnson, S Andreas Zeitler Baurle, S Deme, J Caesar, J Debo, R Fisher, J Wagner, S Lea, S |
| author_sort | Kuhlen, L |
| collection | OXFORD |
| description | Protein secretion through type-three secretion systems (T3SS) is critical for motility and virulence of many bacteria. Proteins are transported through an export gate containing three proteins (FliPQR in flagella, SctRST in virulence systems). A fourth essential T3SS protein (FlhB/SctU) functions to “switch” secretion substrate specificity once the growing hook/needle reach their determined length. Here, we present the cryo-electron microscopy structure of an export gate containing the switch protein from a Vibrio flagellar system at 3.2 Å resolution. The structure reveals that FlhB/SctU extends the helical export gate with its four predicted transmembrane helices wrapped around FliPQR/SctRST. The unusual topology of the FlhB/SctU helices creates a loop wrapped around the bottom of the closed export gate. Structure-informed mutagenesis suggests that this loop is critical in gating secretion and we propose that a series of conformational changes in the T3SS trigger opening of the gate through interactions between FlhB/SctU and FliPQR/SctRST.
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| first_indexed | 2024-03-06T23:43:06Z |
| format | Journal article |
| id | oxford-uuid:6ffe5c13-6132-4899-94d6-f7a1b7bb3f28 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:43:06Z |
| publishDate | 2020 |
| publisher | Nature Research |
| record_format | dspace |
| spelling | oxford-uuid:6ffe5c13-6132-4899-94d6-f7a1b7bb3f282022-03-26T19:34:21ZThe substrate specificity switch FlhB assembles onto the export gate to regulate type three secretionJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6ffe5c13-6132-4899-94d6-f7a1b7bb3f28EnglishSymplectic ElementsNature Research2020Kuhlen, LJohnson, SAndreas ZeitlerBaurle, SDeme, JCaesar, JDebo, RFisher, JWagner, SLea, SProtein secretion through type-three secretion systems (T3SS) is critical for motility and virulence of many bacteria. Proteins are transported through an export gate containing three proteins (FliPQR in flagella, SctRST in virulence systems). A fourth essential T3SS protein (FlhB/SctU) functions to “switch” secretion substrate specificity once the growing hook/needle reach their determined length. Here, we present the cryo-electron microscopy structure of an export gate containing the switch protein from a Vibrio flagellar system at 3.2 Å resolution. The structure reveals that FlhB/SctU extends the helical export gate with its four predicted transmembrane helices wrapped around FliPQR/SctRST. The unusual topology of the FlhB/SctU helices creates a loop wrapped around the bottom of the closed export gate. Structure-informed mutagenesis suggests that this loop is critical in gating secretion and we propose that a series of conformational changes in the T3SS trigger opening of the gate through interactions between FlhB/SctU and FliPQR/SctRST. |
| spellingShingle | Kuhlen, L Johnson, S Andreas Zeitler Baurle, S Deme, J Caesar, J Debo, R Fisher, J Wagner, S Lea, S The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion |
| title | The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion |
| title_full | The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion |
| title_fullStr | The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion |
| title_full_unstemmed | The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion |
| title_short | The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion |
| title_sort | substrate specificity switch flhb assembles onto the export gate to regulate type three secretion |
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