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Three small partner proteins facilitate the type VII-dependent secretion export of an antibacterial nuclease
The type VIIb protein secretion system (T7SSb) plays a role in interbacterial competition in Gram-positive Firmicute bacteria and secretes various toxic effector proteins. The mechanism of secretion and the roles of numerous conserved genes within T7SSb gene clusters remain unknown. EsaD is a nuclea...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10350083/ https://www.ncbi.nlm.nih.gov/pubmed/37461441 http://dx.doi.org/10.1101/2023.04.01.535202 |
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author | Yang, Yaping Boardman, Eleanor Deme, Justin Alcock, Felicity Lea, Susan Palmer, Tracy |
author_facet | Yang, Yaping Boardman, Eleanor Deme, Justin Alcock, Felicity Lea, Susan Palmer, Tracy |
author_sort | Yang, Yaping |
collection | PubMed |
description | The type VIIb protein secretion system (T7SSb) plays a role in interbacterial competition in Gram-positive Firmicute bacteria and secretes various toxic effector proteins. The mechanism of secretion and the roles of numerous conserved genes within T7SSb gene clusters remain unknown. EsaD is a nuclease toxin secreted by the Staphylococcus aureus T7SSb, which forms a complex with its cognate immunity protein, EsaG, and chaperone EsaE. Encoded upstream of EsaD are three small secreted proteins, EsxB, EsxC and EsxD. Here we show that EsxBCD bind to the transport domain of EsaD and function as EsaD export factors. We report the first structural information for a complete T7SSb substrate pre-secretion complex. Cryo-EM of the EsaDEG trimer and the EsaDEG-EsxBCD hexamer shows that incorporation of EsxBCD confers a conformation comprising a flexible globular cargo domain attached to a long narrow shaft that is likely to be crucial for efficient toxin export. |
format | Online Article Text |
id | pubmed-10350083 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Cold Spring Harbor Laboratory |
record_format | MEDLINE/PubMed |
spelling | pubmed-103500832023-07-17 Three small partner proteins facilitate the type VII-dependent secretion export of an antibacterial nuclease Yang, Yaping Boardman, Eleanor Deme, Justin Alcock, Felicity Lea, Susan Palmer, Tracy bioRxiv Article The type VIIb protein secretion system (T7SSb) plays a role in interbacterial competition in Gram-positive Firmicute bacteria and secretes various toxic effector proteins. The mechanism of secretion and the roles of numerous conserved genes within T7SSb gene clusters remain unknown. EsaD is a nuclease toxin secreted by the Staphylococcus aureus T7SSb, which forms a complex with its cognate immunity protein, EsaG, and chaperone EsaE. Encoded upstream of EsaD are three small secreted proteins, EsxB, EsxC and EsxD. Here we show that EsxBCD bind to the transport domain of EsaD and function as EsaD export factors. We report the first structural information for a complete T7SSb substrate pre-secretion complex. Cryo-EM of the EsaDEG trimer and the EsaDEG-EsxBCD hexamer shows that incorporation of EsxBCD confers a conformation comprising a flexible globular cargo domain attached to a long narrow shaft that is likely to be crucial for efficient toxin export. Cold Spring Harbor Laboratory 2023-06-08 /pmc/articles/PMC10350083/ /pubmed/37461441 http://dx.doi.org/10.1101/2023.04.01.535202 Text en https://creativecommons.org/licenses/by/4.0/This work is licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/) , which allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. |
spellingShingle | Article Yang, Yaping Boardman, Eleanor Deme, Justin Alcock, Felicity Lea, Susan Palmer, Tracy Three small partner proteins facilitate the type VII-dependent secretion export of an antibacterial nuclease |
title | Three small partner proteins facilitate the type VII-dependent secretion export of an antibacterial nuclease |
title_full | Three small partner proteins facilitate the type VII-dependent secretion export of an antibacterial nuclease |
title_fullStr | Three small partner proteins facilitate the type VII-dependent secretion export of an antibacterial nuclease |
title_full_unstemmed | Three small partner proteins facilitate the type VII-dependent secretion export of an antibacterial nuclease |
title_short | Three small partner proteins facilitate the type VII-dependent secretion export of an antibacterial nuclease |
title_sort | three small partner proteins facilitate the type vii-dependent secretion export of an antibacterial nuclease |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10350083/ https://www.ncbi.nlm.nih.gov/pubmed/37461441 http://dx.doi.org/10.1101/2023.04.01.535202 |
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