ArticleThe Journal of biological chemistry2014
The polypeptide transport-associated (POTRA) domains of TpsB transporters determine the system specificity of two-partner secretion systems.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- Genomic erosion and horizontal gene transfer shape functional differences of the ExlA toxin iniScience · 2022Article
- Article
- Molecular interactions between Neisseria meningitidis and its human host.Cellular microbiology · 2019Review
- The Growing Genetic and Functional Diversity of Extended Spectrum Beta-Lactamases.BioMed research international · 2018Review
- Cloning, Expression, and Immunogenicity of Fimbrial-F17A Subunit Vaccine againstBioMed research international · 2017Article
- Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions.Frontiers in cellular and infection microbiology · 2017Review
- Biological Functions of the Secretome ofFrontiers in cellular and infection microbiology · 2017Review
- Meningococcal Two-Partner Secretion Systems and Their Association with Outcome in Patients with Meningitis.Infection and immunity · 2016Article
- Fratricide activity of MafB protein of N. meningitidis strain B16B6.BMC microbiology · 2015Article
- Structure-function analysis reveals that the Pseudomonas aeruginosa Tps4 two-partner secretion system is involved in CupB5 translocation.Protein science : a publication of the Protein Society · 2015Article
- A new family of secreted toxins in pathogenic Neisseria species.PLoS pathogens · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The two-partner secretion (TPS) systems of Gram-negative bacteria secrete large TpsA exoproteins by a dedicated TpsB transporter in the outer membrane. TpsBs contain an N-terminal module located in the periplasm that includes two polypeptide transport-associated (POTRA) domains. These are thought to initiate secretion of a TpsA by binding its N-terminal secretion signal, called the TPS domain. Neisseria meningitidis encodes up to five TpsA proteins that are secreted via only two TpsB transporters: TpsB1 and TpsB2. Of these two, the TpsB2 recognizes the TPS domains of all TpsAs, despite their sequence diversity. By contrast, the TpsB1 shows a limited recognition of a TPS domain that is shared by two TpsAs. The difference in substrate specificity of the TpsBs enabled us to investigate the role of the POTRA domains in the selection of TPS domains. We tested secretion of TPS domains or full-length TpsAs by TpsB mutants with deleted, duplicated, and exchanged POTRA domains. Exchanging the two POTRA domains of a TpsB resulted in a switch in specificity. Furthermore, exchanging a single POTRA domain showed that each of the two domains contributed to the cargo selection. Remarkably, the order of the POTRA domains could be reversed without affecting substrate selection, but this aberrant order did result in an alternatively processed secretion product. Our results suggest that secretion of a TpsA is initiated by engaging both POTRA domains of a TpsB transporter and that these select the cognate TpsAs for secretion.
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