Bacterial lipoproteins; biogenesis, sorting and quality control

Narita, Shin‐ichiro; Tokuda, Harukuni

doi:10.1016/j.bbalip.2016.11.009

Cited by 97 publications

(125 citation statements)

References 114 publications

Supporting

Mentioning

114

Contrasting

Unclassified

Order By: Relevance

“…The Bam complex assembles OMPs into the OM (see the recent review (73). Lipoproteins undergo lipid modifications and are extracted from the IM by the LolCDE and passed to the periplasmic chaperone LolA that delivers them to the OM acceptor protein LolB, which inserts lipoproteins into the inner leaflet of the OM (see the recent review (64). …”

Section: Figurementioning

confidence: 99%

Outer Membrane Biogenesis

Konovalova

Kahne²,

Silhavy

2017

Annu. Rev. Microbiol.

247

229

View full text Add to dashboard Cite

The hallmark of Gram-negative bacteria and organelles such as mitochondria and chloroplasts is the presence of an outer membrane (OM). In bacteria such as Escherichia coli, the OM is a unique asymmetric lipid bilayer with lipopolysaccharide (LPS) in the outer leaflet. Integral, transmembrane proteins assume a β-barrel structure (OMPs) and their assembly is catalyzed by the heteropentomeric Bam complex containing the OMP BamA and four lipoproteins, BamB-E. How the Bam complex assembles a great diversity of OMPs into a membrane without an obvious energy source is a particularly challenging problem because folding intermediates are predicted to be unstable in either an aqueous or a hydrophobic environment. Two models have been put forward, the budding model based largely on structural data, and the BamA-assisted model based on genetic and biochemical studies. Here we offer a critical discussion of the pros and cons of each.

show abstract

Section: Figurementioning

confidence: 99%

Outer Membrane Biogenesis

Konovalova

Kahne²,

Silhavy

2017

Annu. Rev. Microbiol.

247

229

View full text Add to dashboard Cite

show abstract

“…ipoproteins are bacterial cell membrane components common throughout Gramnegative and Gram-positive bacteria, constituting 2 to 5% of all cellular proteins (1)(2)(3)(4)(5). Lipoproteins invariably contain a signature acylated N-terminal cysteine residue that tethers an otherwise soluble globular protein domain to the membrane surface.…”

mentioning

confidence: 99%

Identification of the Lyso-Form N -Acyl Intramolecular Transferase in Low-GC Firmicutes

Armbruster

Meredith

2017

J Bacteriol

View full text Add to dashboard Cite

Bacterial lipoproteins are embedded in the cell membrane of both Gram-positive and Gram-negative bacteria, where they serve numerous functions central to cell envelope physiology. Lipoproteins are tethered to the membrane by an N-acyl-S-(mono/di)-acyl-glyceryl-cysteine anchor that is variously acylated depending on the genus. In several low-GC, Gram-positive firmicutes, a monoacyl-glycerylcysteine with an N-terminal fatty acid (known as the lyso form) has been reported, though how it is formed is unknown. Here, through an intergenic complementation rescue assay in Escherichia coli, we report the identification of a common orthologous transmembrane protein in both Enterococcus faecalis and Bacillus cereus that is capable of forming lyso-form lipoproteins. When deleted from the native host, lipoproteins remain diacylated with a free N terminus, as maturation to the N-acylated lyso form is abolished. Evidence is presented suggesting that the previously unknown gene product functions through a novel intramolecular transacylation mechanism, transferring a fatty acid from the diacylglycerol moiety to the ␣-amino group of the lipidated cysteine. As such, the discovered gene has been named lipoprotein intramolecular transacylase (lit), to differentiate it from the gene for the intermolecular N-acyltransferase (lnt) involved in triacyl lipoprotein biosynthesis in Gram-negative organisms.IMPORTANCE This study identifies a new enzyme, conserved among low-GC, Grampositive bacteria, that is involved in bacterial lipoprotein biosynthesis and synthesizes lyso-form lipoproteins. Its discovery is an essential first step in determining the physiological role of N-terminal lipoprotein acylation in Gram-positive bacteria and how these modifications impact bacterial cell envelope function.KEYWORDS firmicutes, acyl transferase, lipoproteins L ipoproteins are bacterial cell membrane components common throughout Gramnegative and Gram-positive bacteria, constituting 2 to 5% of all cellular proteins (1-5). Lipoproteins invariably contain a signature acylated N-terminal cysteine residue that tethers an otherwise soluble globular protein domain to the membrane surface. Positioned at the membrane-environment interface, lipoproteins play critical roles in ion and nutrient capture, solute transport, cell adhesion, and assembly of protein complexes and as protein-folding chaperones.All lipoproteins are initially translated as precursors containing an N-terminal signal peptide harboring a conserved amino acid lipobox motif sequence preceding an invariant cysteine residue (6, 7). Once transported to the outer face of the membrane, prolipoprotein diacylglycerol transferase (Lgt) attaches a diacylglycerol residue from a phospholipid donor through a thioether bond (8). Signal peptidase II (Lsp) then cleaves the leader peptide immediately upstream from the cysteine to liberate the ␣-amino group (9). In Escherichia coli and other Gram-negative bacteria, biosynthesis is completed by an apolipoprotein N-acyltransferase (Lnt), which transfers a...

show abstract

“…This system consists of an ATP-binding cassette (ABC) transporter LolCDE in the inner membrane, a periplasmic chaperone LolA, and LolB, which functions as a receptor in the outer membrane (Figure 3) (for a recent review, see Narita and Tokuda, 2016). The LolCDE complex consists of a heterodimer of two homologous integral membrane proteins, LolC and LolE, which is associated with a dimer of the cytoplasmic ABC protein LolD.…”

Section: Protein Translocation Systems In N Meningitidismentioning

confidence: 99%

Biological Functions of the Secretome of Neisseria meningitidis

Tommassen

Arenas

2017

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Neisseria meningitidis is a Gram-negative bacterial pathogen that normally resides as a commensal in the human nasopharynx but occasionally causes disease with high mortality and morbidity. To interact with its environment, it transports many proteins across the outer membrane to the bacterial cell surface and into the extracellular medium for which it deploys the common and well-characterized autotransporter, two-partner and type I secretion mechanisms, as well as a recently discovered pathway for the surface exposure of lipoproteins. The surface-exposed and secreted proteins serve roles in host-pathogen interactions, including adhesion to host cells and extracellular matrix proteins, evasion of nutritional immunity imposed by iron-binding proteins of the host, prevention of complement activation, neutralization of antimicrobial peptides, degradation of immunoglobulins, and permeabilization of epithelial layers. Furthermore, they have roles in interbacterial interactions, including the formation and dispersal of biofilms and the suppression of the growth of bacteria competing for the same niche. Here, we will review the protein secretion systems of N. meningitidis and focus on the functions of the secreted proteins.

show abstract

Bacterial lipoproteins; biogenesis, sorting and quality control

Cited by 97 publications

References 114 publications

Outer Membrane Biogenesis

Outer Membrane Biogenesis

Identification of the Lyso-Form N -Acyl Intramolecular Transferase in Low-GC Firmicutes

Biological Functions of the Secretome of Neisseria meningitidis

Contact Info

Product

Resources

About