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Cited by 5Bacterial Genetics and BiotechnologyBiochemical and Structural CharacterizationEscherichia coli research studies

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The periplasmic coiled coil formed by the assembly platform proteins PulL and PulM is critical for function of the Klebsiella type II secretion system

Open access
Li, Yuanyuan, Santos-Moreno, Javier, Francetic, Olivera·2023·Research in Microbiology

Published version of a preprint

Abstract

Bacteria use type II secretion systems (T2SS) to secrete to their surface folded proteins that confer diverse functions, from nutrient acquisition to virulence. In the Klebsiella species, T2SS-mediated secretion of pullulanase (PulA) requires assembly of a dynamic filament called the endopilus. The inner membrane assembly platform (AP) subcomplex is essential for endopilus assembly and PulA secretion. AP components PulL and PulM interact with each other through their C-terminal globular domains and transmembrane segments. Here, we investigated the roles of their periplasmic helices, predicted to form a coiled coil, in assembly and function of the PulL-PulM complex. PulL and PulM variants lacking these periplasmic helices were defective for interaction in the bacterial two-hybrid (BACTH) assay. Their functions in PulA secretion and assembly of PulG subunits into endopilus filaments were strongly reduced. Interestingly, deleting the cytoplasmic peptide of PulM nearly abolished the function of variant PulMΔN and its interaction with PulG, but not with PulL, in the BACTH assay. Nevertheless, PulL was specifically proteolyzed in the presence of the PulMΔN variant, suggesting that PulM N-terminal peptide stabilizes PulL in the cytoplasm. We discuss the implications of these results for the T2S endopilus and type IV pilus assembly mechanisms.

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Metadata

Authors
Li, Y., Santos-Moreno, J., & Francetic, O.
Affiliations
Centre National de la Recherche Scientifique (FR)
Venue
Research in Microbiology
Publisher
Elsevier BV
Published
2023-09
Volume
174
Issue
7
Pages
104075
ISSN
  • 0769-2609 (ISSN-L)
  • 0923-2508
OpenAlex
W4367671701
Cited by
5
References
55
Citations by year
2026: 4 · 2025: 1
FWCI
0.83
Type
journal article
Language
en
Open access
Licence
Locations
  • Research in Microbiology (publishedVersion, cc-by-nc-nd)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed (publishedVersion)
  • Repositori digital de la UPF (Universitat Pompeu Fabra) (submittedVersion, cc-by-nc-nd)
  • HAL (submittedVersion, cc-by-nc-nd)
Funders
  • Agence Nationale de la Recherche (ANR‐19, ANR-19-CE11-0020)
  • Eusko Jaurlaritza
  • China Scholarship Council
  • Centre National de la Recherche Scientifique
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Life Sciences › Immunology and Microbiology › Microbiology › Escherichia coli research studies
Keywords
type II secretion system, Klebsiella, pull, protein-protein interaction, proteolysis
MeSH terms
Type II Secretion Systems, Bacterial Proteins, Klebsiella, Membrane Proteins, Peptides

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CoChat. (2026). Citation check: The periplasmic coiled coil formed by the assembly platform proteins PulL and PulM is critical for function of the Klebsiella type II secretion system. https://app.cochat.ai/papers/10.1016/j.resmic.2023.104075
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Li, Y., Santos-Moreno, J., & Francetic, O. (2023). The periplasmic coiled coil formed by the assembly platform proteins PulL and PulM is critical for function of the Klebsiella type II secretion system. Research in Microbiology. https://doi.org/10.1016/j.resmic.2023.104075

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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