PMID:21784935

Citation	Palomino, C, Marín, E and Fernández, LÁ (2011) The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli. J. Bacteriol. 193:5222-30
Abstract	Fimbrial ushers are the largest β-barrel outer membrane proteins (OMPs) known to date, which function in the polymerization of fimbriae and their translocation to the bacterial surface. Folding and assembly of these complex OMPs are not characterized. Here, we investigate the role of periplasmic chaperones (SurA, Skp, DegP, and FkpA) and individual components of the β-barrel assembly machinery (BAM) complex (BamA, BamB, BamC, and BamE) in the folding of the Escherichia coli FimD usher. The FimD level is dramatically reduced (∼30-fold) in a surA null mutant, but a strong cell envelope stress is constitutively activated with upregulation of DegP (∼10-fold). To demonstrate a direct role of SurA, FimD folding was analyzed in a conditional surA mutant in which SurA expression was controlled. In this strain, FimD is depleted from bacteria in parallel to SurA without significant upregulation of DegP. Interestingly, the dependency on SurA is higher for FimD than for other OMPs. We also demonstrate that a functional BAM complex is needed for folding of FimD. In addition, FimD levels were strongly reduced (∼5-fold) in a mutant lacking the accessory lipoprotein BamB. The critical role of BamB for FimD folding was confirmed by complementation and BamB depletion experiments. Similar to SurA dependency, FimD showed a stronger dependency on BamB than OMPs. On the other hand, folding of FimD was only marginally affected in bamC and bamE mutants. Collectively, our results indicate that FimD usher follows the SurA-BamB pathway for its assembly. The preferential use of this pathway for the folding of OMPs with large β-barrels is discussed.
Links	PubMed PMC3187399 Online version:10.1128/JB.05585-11
Keywords	Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Blotting, Western; Carrier Proteins/genetics; Carrier Proteins/metabolism; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Fimbriae Proteins/genetics; Fimbriae Proteins/metabolism; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Lipid-Linked Proteins/genetics; Lipid-Linked Proteins/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Peptidylprolyl Isomerase/genetics; Peptidylprolyl Isomerase/metabolism; Periplasmic Proteins/genetics; Periplasmic Proteins/metabolism; Protein Binding; Protein Folding; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
ECOLI:SURA	involved_in	GO:0050821: protein stabilization	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
ECOLI:SURA		GO:0050821: protein stabilization	ECO:0000315:		P		Fig.2	complete CACAO 7959

References

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