Structural characterization of protein transport by the Type 9 Secretion System
Open accessPreprint — published as 10.1038/s41564-024-01644-7
Abstract
Secretion Systems are protein export machines that enable bacteria to exploit their environment through the release of protein effectors. The Type 9 Secretion System (T9SS) is an essential virulence determinant in the oral pathogens responsible for periodontitis and immune dysfunction. We have trapped and structurally characterised the Type 9 translocon in the process of substrate transport. The active translocon is augmented by a large periplasmic structure incorporating a homologue of the canonical periplasmic chaperone Skp. Substrate proteins bind to a carrier protein within the translocon pore and energy is required to release this substrate-carrier protein complex from the translocon. We infer a unique protein transport mechanism in which a carrier protein is used to pull substrate proteins through the translocon using energy from a trans-envelope power chain.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
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- Authors
- Berks, B., Lauber, F., Deme, J., Liu, X., Kjær, A., Miller, H., Alcock, F., & Lea, S.
- Affiliations
- University of Oxford (GB)
- Corresponding author
- Berks, Ben
- Lea, Susan
- ORCID
- Venue
- Nature Microbiology
- Published
- 2023-11-16
- Volume
- 9
- Issue
- 4
- Pages
- 1089-1102
- ISSN
- 2058-5276 (ISSN-L)
- PMC
- PMC10994853
- OpenAlex
- W4393225380
- Cited by
- 32
- References
- 1
- Citations by year
- 2026: 7 · 2025: 21 · 2024: 4
- FWCI
- 8.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Nature Microbiology (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B)) (submittedVersion, other-oa)
- Digital Access to Libraries (submittedVersion, other-oa)
- Funders
- Wellcome Trust (219477/Z/19/Z, 107929/Z/15/Z, /Z/15/Z)
- National Institutes of Health
- Directorate for Biological Sciences
- Biotechnology and Biological Sciences Research Council (BB/S007474/1)
- H2020 European Research Council (833713)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Keywords
- bacterial protein secretion, Flavobacterium johnsoniae, Bacteroidetes, Skp chaperone, periplasmic chaperone, carrier proteins, substrate binding, secretion mechanism
- MeSH terms
- Bacterial Proteins, Carrier Proteins, Protein Transport, Bacterial Secretion Systems
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