YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in <i>Escherichia coli</i>

Malinverni, Juliana C.; Werner, John C.; Kim, Seokhee; Sklar, Joseph G.; Kahne, Daniel; Misra, Rajeev; Silhavy, Thomas J.

doi:10.1111/j.1365-2958.2006.05211.x

Cited by 278 publications

(395 citation statements)

References 57 publications

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“…The remaining reading frames encode two proteins with a molecular weight below 85 kDa and a yet unknown function. Similar to the observations for the proteobacterial Omp85 protein (11,23,32), the nOmp85 assembles into higher oligomeric complexes in vivo, as determined by non-denaturing SDS-PAGE (Fig. 1B, lanes 2 and 4) and chemical cross-linking (not shown).…”

Section: Methodssupporting

confidence: 84%

Functional and Phylogenetic Properties of the Pore-forming β-Barrel Transporters of the Omp85 Family

Bredemeier

Schlegel

Ertel

et al. 2007

Journal of Biological Chemistry

101

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␤-Barrel-shaped channels of the Omp85 family are involved in the translocation or assembly of proteins of bacterial, mitochondrial, and plastidic outer membranes. We have compared these proteins to understand the evolutionary development of the translocators. We have demonstrated that the proteins from proteobacteria and mitochondria have a pore diameter that is at least five times smaller than found for the Omp85 in cyanobacteria and plastids. This finding can explain why Omp85 from cyanobacteria (but not the homologous protein from proteobacteria) was remodeled to become the protein translocation pore after endosymbiosis. Further, the pore-forming region of the Omp85 proteins is restricted to the C terminus. Based on a phylogenetic analysis we have shown that the pore-forming domain displays a different evolutionary relationship than the N-terminal domain. In line with this, the affinity of the N-terminal domain to the C-terminal region of the Omp85 from plastids and cyanobacteria differs, even though the N-terminal domain is involved in gating of the pore in both groups. We have further shown that the N-terminal domain of nOmp85 takes part in homo-oligomerization. Thereby, the differences in the phylogeny of the two domains are explained by different functional constraints acting on the regions. The poreforming domain, however, is further divided into two functional regions, where the distal C terminus itself forms a dimeric pore. Based on functional and phylogenetic analysis, we suggest an evolutionary scenario that explains the origin of the contemporary translocon.Polypeptide transport and assembly of proteins into or across the outer membrane of endosymbiotic organelles or Gram-negative bacteria depend on ␤-barrel-shaped channels (1-4). One class of these proteins is composed of polypeptide-transporting ␤-barrel (PTB) 6 channels, whose topology was determined by modeling (5-7). PTBs of recent interest are, e.g. outer membrane proteins (which secrete adhesins such as hemagglutinin) (8, 9) and bacterial (1, 7, 10 -12), mitochondrial (Tob55/Sam50) (5, 13, 14), and chloroplast outer membrane proteins (Toc75) (15) of the Omp85 family. The PTBs are partitioned into two functional categories, namely in translocation of precursor proteins across the membrane and in the assembly of outer membrane proteins (3). Furthermore, comparison between chloroplastic, mitochondrial, and bacterial Omp85 protein sequences revealed a high similarity of these PTBs (14,16,17).The PTB Toc75 forms a complex with Toc34, Toc64, and Toc159 (3). A precursor protein-binding site at Toc75 (15, 18), together with the action of Toc159 (19), facilitates the translocation of precursor proteins across the membrane. In contrast, the Omp85 proteins from Neisseria meningitidis, Escherichia coli, and mitochondria are involved in the assembly of outer membrane proteins (1,5,7,(11)(12)(13)(14). As found for Toc75, the mitochondrial PTB is a component of a larger complex with Mas37 (20, 13) and Tob38/Sam35 (21,22).Recently, it was demonstrated that t...

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Section: Methodssupporting

confidence: 84%

Functional and Phylogenetic Properties of the Pore-forming β-Barrel Transporters of the Omp85 Family

Bredemeier

Schlegel

Ertel

et al. 2007

Journal of Biological Chemistry

101

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“…It is unclear how LptE can participate in the assembly of LptD, which is folded at the OM by the β-barrel assembly machine (the Bam complex; [34][35][36][37][38][39]. The fact that LptE contacts a region of LptD important for LptD assembly suggests two possible roles for LptE in this process.…”

Section: Discussionmentioning

confidence: 99%

The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel

Freinkman

Chng

Kahne

2011

Proc. Natl. Acad. Sci. U.S.A.

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158

181

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The cell surfaces of Gram-negative bacteria are composed of lipopolysaccharide (LPS). This glycolipid is found exclusively in the outer leaflet of the asymmetric outer membrane (OM), where it forms a barrier to the entry of toxic hydrophobic molecules into the cell. LPS typically contains six fatty acyl chains and up to several hundred sugar residues. It is biosynthesized in the cytosol and must then be transported across two membranes and an aqueous intermembrane space to the cell surface. These processes are required for the viability of most Gram-negative organisms. The integral membrane β-barrel LptD and the lipoprotein LptE form an essential complex in the OM, which is necessary for LPS assembly. It is not known how this complex translocates large, amphipathic LPS molecules across the OM to the outer leaflet. Here, we show that LptE resides within the LptD β-barrel both in vitro and in vivo. LptD/E associate via an extensive interface; in one specific interaction, LptE contacts a predicted extracellular loop of LptD through the lumen of the β-barrel. Disrupting this interaction site compromises the biogenesis of LptD. This unprecedented two-protein plug-and-barrel architecture suggests how LptD/E can insert LPS from the periplasm directly into the outer leaflet of the OM to establish the asymmetry of the bilayer.lipopolysaccharide assembly | outer membrane protein complex

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“…Lgt is an essential enzyme in Gram-negative bacteria, possibly because of the essential nature of murein lipoprotein and other outer membrane lipoproteins such as YfiO [30], but is dispensable for growth in vitro of all Grampositive bacteria tested to date (see later). Intriguingly, although lgt is present as a single gene in most bacterial genomes, there are two putative lgt paralogues encoded in the genomes of a limited selection of Gram-negative (e.g.…”

Section: Lipoprotein Biogenesismentioning

confidence: 99%

Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold ‘em, knowing when to fold ‘em

Hutchings

Palmer

Harrington

et al. 2009

Trends in Microbiology

181

219

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YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli

Cited by 278 publications

References 57 publications

Functional and Phylogenetic Properties of the Pore-forming β-Barrel Transporters of the Omp85 Family

Functional and Phylogenetic Properties of the Pore-forming β-Barrel Transporters of the Omp85 Family

The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel

Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold ‘em, knowing when to fold ‘em

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