Structure, Function, and Transport of Lipoproteins in<i>Escherichia coli</i>

Tokuda, Harukuni; Matsuyama, Shin-ichi; Tanaka-Masuda, Kimie

doi:10.1128/9781555815806.ch4

Cited by 18 publications

(14 citation statements)

References 57 publications

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“…Some examples of lipid-modified surface-associated proteins in diderm pathogens are Klebsiella oxytoca pullulanase PulA [77], Neisseria gonorrhoeae iron-scavenging proteins LbpB and TbpB [78-80] or peptidyl-prolyl cis/trans isomerase Ng-MIP [81], Porphyromonas gingivalis hemin-binding protein IhtB [82], Vibrio cholerae lipid-scavenging phospholipase VolA [83], Neisseria meningitidis surface protease NalP [84, 85], Bordetella pertussis maturation subtilisin SphB1 [86], Campylobacter jejuni adhesin JlpA, which interestingly has a “catcher’s mitt”-like structure similar to LolB [87, 88], or several Capnocytophaga canimorsus surface lipoproteins associated with glycan foraging systems [89]. In the model organism E. coli, only four of the about 90 lipoproteins [90, 91] have been demonstrated to be at least partially surface exposed [92-95]. In contrast, about two thirds of the over 120 lipoproteins expressed by the spirochetal pathogen Borrelia burgdorferi localize to the surface (S. Chen, A.S. Dowdell, M.D.…”

Section: Secretion Through the Outer Membrane: Rare In Most But Cmentioning

confidence: 99%

Secretion of Bacterial Lipoproteins: Through the Cytoplasmic Membrane, the Periplasm and Beyond

Zückert

2014

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

178

193

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Bacterial lipoproteins are peripherally anchored membrane proteins that play a variety of roles in bacterial physiology and virulence in monoderm (single membrane-enveloped, e.g., grampositive) and diderm (double membrane-enveloped, e.g., gram-negative) bacteria. After export of prolipoproteins through the cytoplasmic membrane, which occurs predominantly but not exclusively via the general secretory or Sec pathway, the proteins are lipid-modified at the cytoplasmic membrane in a multistep process that involves sequential modification of a cysteine residue and cleavage of the signal peptide by the signal II peptidase Lsp. In both monoderms and diderms, signal peptide processing is preceded by acylation with a diacylglycerol through preprolipoprotein diacylglycerol transferase (Lgt). In diderms but also some monoderms, lipoproteins are further modified with a third acyl chain through lipoprotein N-acyl transferase (Lnt). Fully modified lipoproteins that are destined to be anchored in the inner leaflet of the outer membrane (OM) are selected, transported and inserted by the Lol (lipoprotein outer membrane localization) pathway machinery, which consists of the inner-membrane (IM) ABC transporterlike LolCDE complex, the periplasmic LolA chaperone and the OM LolB lipoprotein receptor. Retention of lipoproteins in the cytoplasmic membrane results from Lol avoidance signals that were originally described as the “+2 rule”. Surface localization of lipoproteins in diderms is rare in most bacteria, with the exception of several spirochetal species. Type 2 (T2SS) and type 5 (T5SS) secretion systems are involved in secretion of specific surface lipoproteins of γ-proteobacteria. In the model spirochete Borrelia burgdorferi, surface lipoprotein secretion does not follow established sorting rules, but remains dependent on N-terminal peptide sequences. Secretion through the outer membrane requires maintenance of lipoproteins in a translocation-competent unfolded conformation, likely through interaction with a periplasmic holding chaperone, which delivers the proteins to an outer membrane lipoprotein flippase.

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Section: Secretion Through the Outer Membrane: Rare In Most But Cmentioning

confidence: 99%

Secretion of Bacterial Lipoproteins: Through the Cytoplasmic Membrane, the Periplasm and Beyond

Zückert

2014

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

178

193

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“…The majority of lipoproteins reside in the inner leaflet of the outer membrane (OM) (Tokuda, Matsuyama and Tanaka-Masuda 2007), although recent examples of surface-exposed lipoproteins have been reported (see below). They reach this cellular location by a specific lipoprotein outer membrane localization pathway (Lol) that is composed of five proteins: a cytoplasmic ATP-ase LolD, two cytoplasmic membrane proteins LolC and LolE, a periplasmic chaperone LolA and an OM receptor LolB (Fig.…”

Section: Sorting Of Lipoproteins To the Outer Membranementioning

confidence: 99%

The molecular mechanism of bacterial lipoprotein modification—How, when and why?

Buddelmeijer¹

2015

FEMS Microbiology Reviews

106

117

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One-sentence summary: This review highlights recent findings on the mechanism by which proteins are lipidated and discusses the enzymes involved, substrate specificities among bacterial species and the role of lipoprotein modification in the biogenesis of the cell envelope. Editor: Mecky Pohlschroder ABSTRACTPosttranslational modification of proteins by lipidation is a common process in biological systems. Lipids provide protein stability, interaction with other membrane components, and in some cases, due to reversibility of the process, a mechanism for regulating protein localization and function. Bacterial lipoproteins possess fatty acids at their amino-termini that are derived from phospholipids, and this lipid moiety anchors the proteins into the membrane. These lipids, as is the case for lipopolysaccharides and lipoteichoic acids, play an important role in signaling of the innate immune system through the interaction with Toll-like receptors. Over the past three years, tremendous progress has been made in understanding the mechanism by which lipoproteins become lipidated. Advanced methodology in mass spectrometry, proteomics and genome-wide analyses allowed precise characterization of lipoprotein modifications and the identification of the enzymes catalyzing the reactions in diverse bacterial species. This review will highlight new findings on bacterial lipoprotein modification with focus on the reaction mechanisms and the role of lipoproteins in cell envelope homeostasis.

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“…The yfgC promoter is regulated by sigma E, i.e., protein folding stress (23,57), and yfgC mutants are hypersensitive toward multiple antibiotics (24,38). The other M48 family members, YcaL and YggG, are outer membrane lipoproteins (37,69). The yggG promoter is upregulated by heat shock (28) and by the Rcs two-component system (25), while insertions within the ycaL gene are lethal in Salmonella enterica (32) but not in E. coli.…”

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confidence: 99%

Genetic Analysis of 15 Protein Folding Factors and Proteases of the Escherichia coli Cell Envelope

Weski

Ehrmann

2012

J Bacteriol

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Each cell hosts thousands of proteins that vary greatly in abundance, structure, and chemical properties. To ensure that all proteins are biologically active and properly localized, efficient quality control systems have evolved. While the structure, function, and regulation of some individual protein folding factors and proteases were resolved up to atomic resolution, others remain poorly characterized. In addition, little is known about which factors are required for viability under specific stress conditions. We therefore determined the physiological implications of 15 factors of the E. coli cell envelope by an integrated genetic approach comprising phenotypic analyses. Our data indicate that surA and tsp null mutations are a lethal combination in rich medium, that surA dsbA and surA dsbC double mutants are temperature sensitive, and that surA ptrA , surA yfgC , dsbA fkpA , degP tsp , degP ppiD , tsp ppiD , and degP dsbA double mutants are temperature sensitive in rich medium containing 0.5 M NaCl, while degP dsbA , degP yfgC , tsp ydgD , and degP tsp double mutants do not grow in the presence of SDS/EDTA. Furthermore, we show that in degP dsbA , degP tsp , and degP yfgC double mutants a subpopulation of LamB exists as unfolded monomers. In addition, dsbA null mutants expressed lower levels of the outer membrane proteins LptD, LamB, FhuA, and OmpW while FhuA levels were reduced in surA single and degP ppiD double mutants. Lower FhuA levels in degP ppiD strains depend on Tsp, since in a tsp degP ppiD triple mutant FhuA levels are restored.

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Structure, Function, and Transport of Lipoproteins inEscherichia coli

Cited by 18 publications

References 57 publications

Secretion of Bacterial Lipoproteins: Through the Cytoplasmic Membrane, the Periplasm and Beyond

Secretion of Bacterial Lipoproteins: Through the Cytoplasmic Membrane, the Periplasm and Beyond

The molecular mechanism of bacterial lipoprotein modification—How, when and why?

Genetic Analysis of 15 Protein Folding Factors and Proteases of the Escherichia coli Cell Envelope

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