Hemin- and temperature-dependent proteome alteration of Porphyromonas gingivalis - DIA
Ontology highlight
ABSTRACT:
INSTRUMENT(S):
ORGANISM(S): Bacteria Porphyromonas Gingivalis Atcc 33277
DISEASE(S): Periodontitis
SUBMITTER: 
Tianfan Cheng
LAB HEAD: Lijian Jin
PROVIDER: PXD057093 | Pride | 2026-02-21
REPOSITORIES: Pride
Dataset's files
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|---|---|---|---|---|
| 21P04410001.raw | Raw | |||
| 21P04410002.raw | Raw | |||
| 21P04410003.raw | Raw | |||
| 21P04410004.raw | Raw | |||
| 21P04410005.raw | Raw |
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Project description:The BAM (b-barrel assembly machinery) complex is an evolutionarily conserved, multiprotein machine that catalyses the folding and membrane insertion of newly synthesised b-barrel outer membrane (OM) proteins in Gram-negative bacteria, mitochondria and chloroplasts. Based on Proteobacteria, bacterial BAM is also structurally conserved, with an essential BamAD core and up to three auxilliary periplasmic lipoproteins of poorly defined function. Here we show, using structural biology, quantitative proteomics and functional assays, that the BAM complex is radically different within the Bacteroidetes, a large and important phylum widely distributed within the environment and animal microbiomes. Cryogenic electron microscopy (cryoEM) structures of the BAM complexes from the human gut symbiont Bacteroides thetaiotaomicron and the human oral pathogen Porphyromonas gingivalis show similar, seven-component complexes of ~325 kDa in size with most of the mass in the extracellular space. In addition to canonical BamA and BamD, the complexes contain an integral OM protein named BamF that is essential and intimately associated with BamA, plus four surface-exposed lipoproteins (SLPs) named BamG-J. Together, BamF-J form a large, extracellular dome that likely serves as an assembly cage for the b-barrel-SLP complexes that are a hallmark of the Bacteroidetes. Our data suggest that BAM functionality in Bacteroidetes is substantially extended from that in Proteobacteria and underscores the importance of studying non-Proteobacteria for a more complete understanding of fundamental biological processes.
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Project description:The BAM (b-barrel assembly machinery) complex is an evolutionarily conserved, multiprotein machine that catalyses the folding and membrane insertion of newly synthesised b-barrel outer membrane (OM) proteins in Gram-negative bacteria, mitochondria and chloroplasts. Based on Proteobacteria, bacterial BAM is also structurally conserved, with an essential BamAD core and up to three auxilliary periplasmic lipoproteins of poorly defined function. Here we show, using structural biology, quantitative proteomics and functional assays, that the BAM complex is radically different within the Bacteroidetes, a large and important phylum widely distributed within the environment and animal microbiomes. Cryogenic electron microscopy (cryoEM) structures of the BAM complexes from the human gut symbiont Bacteroides thetaiotaomicron and the human oral pathogen Porphyromonas gingivalis show similar, seven-component complexes of ~325 kDa in size with most of the mass in the extracellular space. In addition to canonical BamA and BamD, the complexes contain an integral OM protein named BamF that is essential and intimately associated with BamA, plus four surface-exposed lipoproteins (SLPs) named BamG-J. Together, BamF-J form a large, extracellular dome that likely serves as an assembly cage for the b-barrel-SLP complexes that are a hallmark of the Bacteroidetes. Our data suggest that BAM functionality in Bacteroidetes is substantially extended from that in Proteobacteria and underscores the importance of studying non-Proteobacteria for a more complete understanding of fundamental biological processes.
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