The assembly of β-barrel outer membrane proteins

Tomasek, David; Kahne, Daniel

doi:10.1016/j.mib.2021.01.009

Cited by 59 publications

(52 citation statements)

References 50 publications

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“…T5SS proteins exported by the Sec translocon emerge in the periplasm, with their N-terminus first, in an unfolded conformation. The translocator domains must then reach the outer membrane, in which they are inserted/folded by the BAM (β-barrel assembly machinery) or TAM (translocation and assembly module) machineries [ 85 , 86 , 87 ]. Meanwhile, the long passenger domains must be prevented from aggregation and degradation and maintained in a conformation competent for proper translocation across the OM.…”

Section: Periplasmic Transitmentioning

confidence: 99%

“…In 2003, a conserved system essential for the insertion and folding of β-barrel proteins in the outer membrane of Gram-negative bacteria was discovered [ 33 ]. Since then, the now-called BAM (β-barrel assembly machinery) complex has been extensively studied both biochemically and structurally [ 33 , 85 , 86 ].…”

Section: Translocator Domain Insertion and Folding In The Outer Membranementioning

confidence: 99%

“…Although the mechanism by which BAM inserts and folds β-barrels in the OM is not completely deciphered [ 34 , 85 , 86 , 143 ], structural studies have indicated that BamA can adopt multiple conformations, with its N- and C-terminal β-strands pairing either via 8 (closed barrel) or only 2 (open barrel) hydrogen bonds [ 135 , 136 , 137 , 138 , 139 ]. It was hence proposed that the substrate terminal β-strands could pair with the BamA lateral seam to initiate β-sheet formation in the OM.…”

Section: Translocator Domain Insertion and Folding In The Outer Membranementioning

confidence: 99%

“…It was hence proposed that the substrate terminal β-strands could pair with the BamA lateral seam to initiate β-sheet formation in the OM. This led to a “budding” model in which the substrate β-barrel forms a hybrid barrel with BamA and buds out in the membrane once folding is complete [ 85 , 86 , 135 , 143 ]. This model is supported by the recent observation, by cryo-electron microscopy, of such a hybrid barrel formed between BamA and a substrate [ 144 ].…”

Section: Translocator Domain Insertion and Folding In The Outer Membranementioning

confidence: 99%

“…How the b-barrels are finally released into the OM is less clear [ 86 ].…”

Section: Translocator Domain Insertion and Folding In The Outer Membranementioning

confidence: 99%

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Folding Control in the Path of Type 5 Secretion

Dautin

2021

Toxins

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The type 5 secretion system (T5SS) is one of the more widespread secretion systems in Gram-negative bacteria. Proteins secreted by the T5SS are functionally diverse (toxins, adhesins, enzymes) and include numerous virulence factors. Mechanistically, the T5SS has long been considered the simplest of secretion systems, due to the paucity of proteins required for its functioning. Still, despite more than two decades of study, the exact process by which T5SS substrates attain their final destination and correct conformation is not totally deciphered. Moreover, the recent addition of new sub-families to the T5SS raises additional questions about this secretion mechanism. Central to the understanding of type 5 secretion is the question of protein folding, which needs to be carefully controlled in each of the bacterial cell compartments these proteins cross. Here, the biogenesis of proteins secreted by the Type 5 secretion system is discussed, with a focus on the various factors preventing or promoting protein folding during biogenesis.

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Section: Periplasmic Transitmentioning

confidence: 99%

Section: Translocator Domain Insertion and Folding In The Outer Membranementioning

confidence: 99%

Section: Translocator Domain Insertion and Folding In The Outer Membranementioning

confidence: 99%

Section: Translocator Domain Insertion and Folding In The Outer Membranementioning

confidence: 99%

“…How the b-barrels are finally released into the OM is less clear [ 86 ].…”

Section: Translocator Domain Insertion and Folding In The Outer Membranementioning

confidence: 99%

See 3 more Smart Citations

Folding Control in the Path of Type 5 Secretion

Dautin

2021

Toxins

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ATP‐independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next‐generation therapeutics

George,

Patil,

Mahalakshmi

2024

Protein Science

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Diderm bacteria employ β‐barrel outer membrane proteins (OMPs) as their first line of communication with their environment. These OMPs are assembled efficiently in the asymmetric outer membrane by the β‐Barrel Assembly Machinery (BAM). The multi‐subunit BAM complex comprises the transmembrane OMP BamA as its functional subunit, with associated lipoproteins (e.g., BamB/C/D/E/F, RmpM) varying across phyla and performing different regulatory roles. The ability of BAM complex to recognize and fold OM β‐barrels of diverse sizes, and reproducibly execute their membrane insertion, is independent of electrochemical energy. Recent atomic structures, which captured BAM–substrate complexes, show the assembly function of BamA can be tailored, with different substrate types exhibiting different folding mechanisms. Here, we highlight common and unique features of its interactome. We discuss how this conserved protein complex has evolved the ability to effectively achieve the directed assembly of diverse OMPs of wide‐ranging sizes (8–36 β‐stranded monomers). Additionally, we discuss how darobactin—the first natural membrane protein inhibitor of Gram‐negative bacteria identified in over five decades—selectively targets and specifically inhibits BamA. We conclude by deliberating how a detailed deduction of BAM complex—associated regulation of OMP biogenesis and OM remodeling will open avenues for the identification and development of effective next‐generation therapeutics against Gram‐negative pathogens.

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Monitoring the Interaction of the Peptidoglycan with the Bacterial β-Barrel Assembly Machinery

Corona,

Vollmer

2024

Methods in Molecular Biology

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The assembly of β-barrel outer membrane proteins

Cited by 59 publications

References 50 publications

Folding Control in the Path of Type 5 Secretion

Folding Control in the Path of Type 5 Secretion

ATP‐independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next‐generation therapeutics

Monitoring the Interaction of the Peptidoglycan with the Bacterial β-Barrel Assembly Machinery

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