The bacterial outer membrane β‐barrel assembly machinery

Kim, Kelly H.; Aulakh, Suraaj; Paetzel, Mark

doi:10.1002/pro.2069

Cited by 104 publications

(119 citation statements)

References 107 publications

Supporting

Mentioning

116

Contrasting

Order By: Relevance

“…Furthermore, in the outer membrane of mitochondria, a similar integrated supercomplex, containing the translocase of the outer membrane (TOM) and the sorting and assembly machinery (SAM, a homolog of the BAM complex), was reported to function in mitochondrial ␤-barrel OMP biogenesis (31). In chloroplasts, ␤-barrel OMP biogenesis involves the outer membrane translocon TOC, the inner membrane translocon TIC, and the assembly protein Toc-75V, a homolog of bacterial BamA (11). The question of whether a similar integrated supercomplex is also formed in chloroplasts certainly merits further investigation.…”

Section: Discussionmentioning

confidence: 99%

“…The ␤-barrel OMP assembly machine (i.e. the BAM complex) protein BamA, which has homologues in mitochondria (designated as Sam50) and chloroplasts (designated as Toc75), consists of a ␤-barrel domain that is integrated in the outer membrane and a POTRA (polypeptide translocation-associated) domain that extends into the periplasmic space (11). Genetic and biochemical observations showed that BamA is essential for the folding and membrane insertion of ␤-barrel OMPs (5,9,12,13).…”

mentioning

confidence: 99%

See 1 more Smart Citation

A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria

Wang

Feng

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

␤-barrel outer membrane proteins (OMPs) are ubiquitously present in Gram-negative bacteria, mitochondria and chloroplasts, and function in a variety of biological processes. The mechanism by which the hydrophobic nascent ␤-barrel OMPs are transported through the hydrophilic periplasmic space in bacterial cells remains elusive. Here, mainly via unnatural amino acid-mediated in vivo photo-crosslinking studies, we revealed that the primary periplasmic chaperone SurA interacts with nascent ␤-barrel OMPs largely via its N-domain but with ␤-barrel assembly machine protein BamA mainly via its satellite P2 domain, and that the nascent ␤-barrel OMPs interact with SurA via their N-and C-terminal regions. Additionally, via dual in vivo photo-crosslinking, we demonstrated the formation of a ternary complex involving ␤-barrel OMP, SurA, and BamA in cells. More importantly, we found that a supercomplex spanning the inner and outer membranes and involving the BamA, BamB, SurA, PpiD, SecY, SecE, and SecA proteins appears to exist in living cells, as revealed by a combined analyses of sucrose-gradient ultra-centrifugation, Blue native PAGE and mass spectrometry. We propose that this supercomplex integrates the translocation, transportation, and membrane insertion events for ␤-barrel OMP biogenesis.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria

Wang

Feng

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…One of the unique features of the outer membrane of Gramnegative bacteria-as well as those of mitochondria and chloroplasts-is its high content of b-barrel outer membrane proteins (OMPs) [10][11][12][13][14][15] . In bacteria, the biogenesis of b-barrel OMPs depends on the b-barrel assembly machinery (BAM), which in g-proteobacteria is composed of five components, named BamA-E.…”

mentioning

confidence: 99%

“…In bacteria, the biogenesis of b-barrel OMPs depends on the b-barrel assembly machinery (BAM), which in g-proteobacteria is composed of five components, named BamA-E. The central BAM component, BamA, itself is a b-barrel protein that belongs to the Omp85 family [10][11][12][13][14][15] . Omp85 family members function in the intramembrane formation of bbarrels, while another group, represented by the above-mentioned TpsB proteins, facilitates translocation of the TpsA passenger proteins across the outer membrane.…”

mentioning

confidence: 99%

Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins

et al. 2014

View full text Add to dashboard Cite

Gram-negative bacteria use the type-V secretion pathway to expose proteins at their cell surface, many of which have virulence functions. Translocation of those proteins across the outer membrane occurs either by means of dedicated translocator proteins (two-partner secretion) or covalently fused translocator domains (autotransporters). Translocator proteins and translocator domains are b-barrels requiring the b-barrel assembly machinery (BAM) for membrane integration. However, the molecular details of their passage across the envelope and insertion into the outer membrane remain enigmatic, owing in part to the fact that in vitro systems are not available. Here we describe a versatile in vitro reconstitution system that faithfully reproduces both branches of the type-V secretion pathway and the assembly of b-barrel outer membrane proteins. This system will allow an in-depth analysis of protein secretion across and integration into outer membranes.

show abstract

“…This asymmetric phospholipid and lipopolysaccharide (LPS) bilayer also acts as a scaffold for two major classes of membrane proteins: the integral outer membrane proteins (OMPs) and the lipoproteins (3). Integral OMPs are often referred to as ␤-barrel proteins and are assembled into the OM by the ␤-barrel assembly machinery (BAM) (4,5,6,7,8,9). The BAM complex is composed of five proteins: BamA, which is itself an integral OMP, and the four lipoproteins BamB, BamC, BamD, and BamE, which localize to the inner leaflet of the OM (5,6).…”

mentioning

confidence: 99%

Demarcating SurA Activities Required for Outer Membrane Targeting of Yersinia pseudotuberculosis Adhesins

Obi

Francis

2013

Infect Immun

View full text Add to dashboard Cite

SurA is a periplasmic protein folding factor involved in chaperoning and trafficking of outer membrane proteins across the Gram-negative bacterial periplasm. In addition, SurA also possesses peptidyl-prolyl cis/trans isomerase activity. We have previously reported that in enteropathogenic Yersinia pseudotuberculosis, SurA is needed for bacterial virulence and envelope integrity. In this study, we investigated the role of SurA in the assembly of important Yersinia adhesins. Using genetic mutation, biochemical characterization, and an in vitro-based bacterial host cell association assay, we confirmed that surface localization of the invasin adhesin is dependent on SurA. As a surA deletion also has some impact on the levels of individual components of the BAM complex in the Yersinia outer membrane, abolished invasin surface assembly could reflect both a direct loss of SurA-dependent periplasmic targeting and a potentially compromised BAM complex assembly platform in the outer membrane. To various degrees, the assembly of two other adhesins, Ail and the pH 6 antigen fibrillum PsaA, also depends on SurA. Consequently, loss of SurA leads to a dramatic reduction in Yersinia attachment to eukaryotic host cells. Genetic complementation of surA deletion mutants indicated a prominent role for SurA chaperone function in outer membrane protein assembly. Significantly, the N terminus of SurA contributed most of this SurA chaperone function. Despite a dominant chaperoning role, it was also evident that SurA isomerization activity did make a modest contribution to this assembly process.

show abstract

The bacterial outer membrane β‐barrel assembly machinery

Cited by 104 publications

References 107 publications

A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria

A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria

Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins

Demarcating SurA Activities Required for Outer Membrane Targeting of Yersinia pseudotuberculosis Adhesins

Contact Info

Product

Resources

About