PXD056806

PXD056806 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2024-10-15 00:49:40	ID requested
⏵ 1	2025-03-11 01:57:00	announced

10.1016/J.JMB.2025.169063;

10.6019/PXD056806;

submitter keyword: membrane vesicles,TAM complex, proteomics, lipidomics, LC-MS, Bacteroidetes, outer membrane, lipoproteins

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

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PRIDE project URI

• PRIDE
  1. PXD056806
     1. Label: PRIDE project
     2. Name: TamL is a key player of the outer membrane homeostasis in Bacteroidetes.