Glycine acylation and trafficking of a new class of bacterial lipoprotein by a composite secretion system
Protein acylation is critical for many cellular functions across all domains of life. In bacteria, lipoproteins have important roles in virulence and are targets for the development of antimicrobials and vaccines. Bacterial lipoproteins are secreted from the cytosol via the Sec pathway and acylated...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2021-02-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/63762 |
| _version_ | 1811180556846628864 |
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| author | Christopher Icke Freya J Hodges Karthik Pullela Samantha A McKeand Jack Alfred Bryant Adam F Cunningham Jeff A Cole Ian R Henderson |
| author_facet | Christopher Icke Freya J Hodges Karthik Pullela Samantha A McKeand Jack Alfred Bryant Adam F Cunningham Jeff A Cole Ian R Henderson |
| author_sort | Christopher Icke |
| collection | DOAJ |
| description | Protein acylation is critical for many cellular functions across all domains of life. In bacteria, lipoproteins have important roles in virulence and are targets for the development of antimicrobials and vaccines. Bacterial lipoproteins are secreted from the cytosol via the Sec pathway and acylated on an N-terminal cysteine residue through the action of three enzymes. In Gram-negative bacteria, the Lol pathway transports lipoproteins to the outer membrane. Here, we demonstrate that the Aat secretion system is a composite system sharing similarity with elements of a type I secretion systems and the Lol pathway. During secretion, the AatD subunit acylates the substrate CexE on a highly conserved N-terminal glycine residue. Mutations disrupting glycine acylation interfere with membrane incorporation and trafficking. Our data reveal CexE as the first member of a new class of glycine-acylated lipoprotein, while Aat represents a new secretion system that displays the substrate lipoprotein on the cell surface. |
| first_indexed | 2024-04-11T09:05:19Z |
| format | Article |
| id | doaj.art-b09b42d7284d412aa5219c5349c608ba |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T09:05:19Z |
| publishDate | 2021-02-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-b09b42d7284d412aa5219c5349c608ba2022-12-22T04:32:39ZengeLife Sciences Publications LtdeLife2050-084X2021-02-011010.7554/eLife.63762Glycine acylation and trafficking of a new class of bacterial lipoprotein by a composite secretion systemChristopher Icke0https://orcid.org/0000-0002-7815-8591Freya J Hodges1Karthik Pullela2Samantha A McKeand3Jack Alfred Bryant4https://orcid.org/0000-0002-7912-2144Adam F Cunningham5Jeff A Cole6Ian R Henderson7https://orcid.org/0000-0002-9954-4977Institute for Molecular Bioscience, University of Queensland, Brisbane, AustraliaInstitute for Molecular Bioscience, University of Queensland, Brisbane, AustraliaInstitute for Molecular Bioscience, University of Queensland, Brisbane, AustraliaInstitute of Microbiology and Infection, Birmingham, United KingdomInstitute of Microbiology and Infection, Birmingham, United KingdomInstitute of Microbiology and Infection, Birmingham, United Kingdom; Institute of Immunology and Immunotherapy, University of Birmingham, Birmingham, United KingdomInstitute of Microbiology and Infection, Birmingham, United KingdomInstitute for Molecular Bioscience, University of Queensland, Brisbane, AustraliaProtein acylation is critical for many cellular functions across all domains of life. In bacteria, lipoproteins have important roles in virulence and are targets for the development of antimicrobials and vaccines. Bacterial lipoproteins are secreted from the cytosol via the Sec pathway and acylated on an N-terminal cysteine residue through the action of three enzymes. In Gram-negative bacteria, the Lol pathway transports lipoproteins to the outer membrane. Here, we demonstrate that the Aat secretion system is a composite system sharing similarity with elements of a type I secretion systems and the Lol pathway. During secretion, the AatD subunit acylates the substrate CexE on a highly conserved N-terminal glycine residue. Mutations disrupting glycine acylation interfere with membrane incorporation and trafficking. Our data reveal CexE as the first member of a new class of glycine-acylated lipoprotein, while Aat represents a new secretion system that displays the substrate lipoprotein on the cell surface.https://elifesciences.org/articles/63762lipoproteinacylationn-palmitoylationprotein secretionacyltransferase |
| spellingShingle | Christopher Icke Freya J Hodges Karthik Pullela Samantha A McKeand Jack Alfred Bryant Adam F Cunningham Jeff A Cole Ian R Henderson Glycine acylation and trafficking of a new class of bacterial lipoprotein by a composite secretion system eLife lipoprotein acylation n-palmitoylation protein secretion acyltransferase |
| title | Glycine acylation and trafficking of a new class of bacterial lipoprotein by a composite secretion system |
| title_full | Glycine acylation and trafficking of a new class of bacterial lipoprotein by a composite secretion system |
| title_fullStr | Glycine acylation and trafficking of a new class of bacterial lipoprotein by a composite secretion system |
| title_full_unstemmed | Glycine acylation and trafficking of a new class of bacterial lipoprotein by a composite secretion system |
| title_short | Glycine acylation and trafficking of a new class of bacterial lipoprotein by a composite secretion system |
| title_sort | glycine acylation and trafficking of a new class of bacterial lipoprotein by a composite secretion system |
| topic | lipoprotein acylation n-palmitoylation protein secretion acyltransferase |
| url | https://elifesciences.org/articles/63762 |
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