ArticleBMC molecular and cell biology2019
Remote homology searches identify bacterial homologues of eukaryotic lipid transfer proteins, including Chorein-N domains in TamB and AsmA and Mdm31p.
Article in BMC molecular and cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 57 citations in OpenAlex.
- Mechanism of phospholipid transport to the bacterial outer membrane by TAM.bioRxiv : the preprint server for biology · 2026Article
- The molecular mechanism of lipid uptake by membrane-anchored bridge-like lipid transfer proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural basis of outer membrane biogenesis by the TamAB translocase.Nature communications · 2026Article
- BLTP3A is associated with membranes of the late endocytic pathway and is an effector of CASM.The EMBO journal · 2025Article
- Structure-function relationship of the Pseudomonas aeruginosa AsmA-like proteins YhdP and YdbH involved in outer membrane biogenesis.Protein science : a publication of the Protein Society · 2025Article
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- Inhibiting Lipopolysaccharide Biogenesis: The More You Know the Further You Go.Annual review of biochemistry · 2025Review
- The Extended Synaptotagmins ofPlants (Basel, Switzerland) · 2025Review
- VPS13 and bridge-like lipid transporters, mechanisms, and mysteries.Frontiers in neuroscience · 2025Review
- Redundant essentiality of AsmA-like proteins inmSphere · 2024Article
- Beclin-1: a therapeutic target at the intersection of autophagy, immunotherapy, and cancer treatment.Frontiers in immunology · 2024Review
- Phospholipid transport to the bacterial outer membrane through an envelope-spanning bridge.bioRxiv : the preprint server for biology · 2023Article
- Autophagy genes in biology and disease.Nature reviews. Genetics · 2023Review
- Large-scale phylogenomics of aquatic bacteria reveal molecular mechanisms for adaptation to salinity.Science advances · 2023Article
- Article
- In silico modeling human VPS13 proteins associated with donor and target membranes suggests lipid transfer mechanisms.Proteins · 2023Article
- Cracking outer membrane biogenesis.Biochimica et biophysica acta. Molecular cell research · 2023Article
- Three bacterial DedA subfamilies with distinct functions and phylogenetic distribution.bioRxiv : the preprint server for biology · 2023Article
- A novel superfamily of bridge-like lipid transfer proteins.Trends in cell biology · 2022Review
- Lipid Transport Across Bacterial Membranes.Annual review of cell and developmental biology · 2022Review
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Abstract
backgroundAll cells rely on lipids for key functions. Lipid transfer proteins allow lipids to exit the hydrophobic environment of bilayers, and cross aqueous spaces. One lipid transfer domain fold present in almost all eukaryotes is the TUbular LIPid binding (TULIP) domain. Three TULIP families have been identified in bacteria (P47, OrfX2 and YceB), but their homology to eukaryotic proteins is too low to specify a common origin. Another recently described eukaryotic lipid transfer domain in VPS13 and ATG2 is Chorein-N, which has no known bacterial homologues. There has been no systematic search for bacterial TULIPs or Chorein-N domains.
resultsRemote homology predictions for bacterial TULIP domains using HHsearch identified four new TULIP domains in three bacterial families. DUF4403 is a full length pseudo-dimeric TULIP with a 6 strand β-meander dimer interface like eukaryotic TULIPs. A similar sheet is also present in YceB, suggesting it homo-dimerizes. TULIP domains were also found in DUF2140 and in the C-terminus DUF2993. Remote homology predictions for bacterial Chorein-N domains identified strong hits in the N-termini of AsmA and TamB in diderm bacteria, which are related to Mdm31p in eukaryotic mitochondria. The N-terminus of DUF2993 has a Chorein-N domain adjacent to its TULIP domain.
conclusionsTULIP lipid transfer domains are widespread in bacteria. Chorein-N domains are also found in bacteria, at the N-terminus of multiple proteins in the intermembrane space of diderms (AsmA, TamB and their relatives) and in Mdm31p, a protein that is likely to have evolved from an AsmA/TamB-like protein in the endosymbiotic mitochondrial ancestor. This indicates that both TULIP and Chorein-N lipid transfer domains may have originated in bacteria.
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