| Title: |
Assembly mechanism of a Tad secretion system secretin-pilotin complex |
| Authors: |
Tassinari, Matteo; Rudzite, Marta; Filloux, Alain; Low, Harry H. |
| Contributors: |
Singapore Centre for Environmental Life Sciences and Engineering |
| Publication Year: |
2023 |
| Collection: |
DR-NTU (Digital Repository at Nanyang Technological University, Singapore) |
| Subject Terms: |
Science::Biological sciences; Bacterial Secretion Systems; Cell Aggregation |
| Description: |
The bacterial Tight adherence Secretion System (TadSS) assembles surface pili that drive cell adherence, biofilm formation and bacterial predation. The structure and mechanism of the TadSS is mostly unknown. This includes characterisation of the outer membrane secretin through which the pilus is channelled and recruitment of its pilotin. Here we investigate RcpA and TadD lipoprotein from Pseudomonas aeruginosa. Light microscopy reveals RcpA colocalising with TadD in P. aeruginosa and when heterologously expressed in Escherichia coli. We use cryogenic electron microscopy to determine how RcpA and TadD assemble a secretin channel with C13 and C14 symmetries. Despite low sequence homology, we show that TadD shares a similar fold to the type 4 pilus system pilotin PilF. We establish that the C-terminal four residues of RcpA bind TadD - an interaction essential for secretin formation. The binding mechanism between RcpA and TadD appears distinct from known secretin-pilotin pairings in other secretion systems. ; Published version ; This work was funded by a Wellcome Trust Senior Research Fellowship (215553/Z/19/Z) to HL. |
| Document Type: |
article in journal/newspaper |
| File Description: |
application/pdf |
| Language: |
English |
| Relation: |
Nature Communications; https://hdl.handle.net/10356/171522; 14; 5643 |
| DOI: |
10.1038/s41467-023-41200-1 |
| Availability: |
https://hdl.handle.net/10356/171522; https://doi.org/10.1038/s41467-023-41200-1 |
| Rights: |
© 2023 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/ licenses/by/4.0/. |
| Accession Number: |
edsbas.3198B5 |
| Database: |
BASE |