PXD056806 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | TamL is a key player of the outer membrane homeostasis in Bacteroidetes. |
Description | In Proteobacteria, the outer membrane protein TamA and the inner membrane-anchored protein TamB form the Translocation and Assembly Module (TAM) complex, which facilitates the transport of autotransporters, virulence factors, and likely lipids across the two membranes. In Bacteroidetes, TamB co-occurs with TamL, a TamA-like lipoprotein with a lipid modification at its N-terminus that likely anchors it to the outer membrane. This structural difference suggests that TamL may have a distinct function compared to the TamA homologue in Proteobacteria. However, the role of TAM in bacterial phyla other than Proteobacteria remains unexplored. Our study aimed to elucidate the functional importance of TamL in Flavobacterium johnsoniae, an environmental Bacteroidetes. Unlike its homologues in Proteobacteria, we found that TamL and TamB are essential in F. johnsoniae. Through genetic, phenotypic, proteomic, and lipidomic analyses, we discovered that TamL depletion severely compromises outer membrane integrity, as evidenced by reduced cell viability, altered cell shape, increased susceptibility to membrane-disrupting agents, and elevated levels of outer membrane lipoproteins. Notably, we did not observe any impact on outer membrane lipid composition. Via pull-down protein assays, we confirmed that TamL interacts with TamB in F. johnsoniae, likely forming the TAM complex. Furthermore, our in silico analysis revealed that the presence of TamL and TamB monocistronic genes is a shared genetic feature among Bacteroidetes members, including the human pathogen Capnocytophaga canimorsus where we confirmed the essentiality of the TamL and TamB homologs. To our knowledge, this study is the first to provide functional insights into a TAM subunit beyond Proteobacteria. |
HostingRepository | PRIDE |
AnnounceDate | 2025-03-11 |
AnnouncementXML | Submission_2025-03-11_01:57:00.448.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD056806 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Marc Dieu |
SpeciesList | scientific name: Flavobacterium johnsoniae; NCBI TaxID: 986; |
ModificationList | acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | timsTOF Pro |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-10-15 00:49:40 | ID requested | |
⏵ 1 | 2025-03-11 01:57:00 | announced | |
Publication List
Keyword List
submitter keyword: membrane vesicles,TAM complex, proteomics, lipidomics, LC-MS, Bacteroidetes, outer membrane, lipoproteins |
Contact List
Francesco Renzi |
contact affiliation | Research Unit in Biology of Microorganisms (URBM), Namur Research Institute for life Sciences (Narilis), University of Namur, Namur, Belgium |
contact email | francesco.renzi@unamur.be |
lab head | |
Marc Dieu |
contact affiliation | University of Namur - MaSUN |
contact email | marc.dieu@unamur.be |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD056806
- Label: PRIDE project
- Name: TamL is a key player of the outer membrane homeostasis in Bacteroidetes.