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Bacterial lipoproteins

Up to now, the pectinolytic enzymes of E. chrysanthemi that have been detected were extracellular secreted enzymes (PelA, B, C, D, E, L, exo-Peh and PemA), periplasmic (exo-Pel), or cytoplasmic (OGL) proteins (1, 5). In contrast, PemB is an outer membrane pectinolytic enzyme. To our knowledge it is the first pectinase characterised as a membrane protein. We presented several lines of evidence showing that PemB is a lipoprotein (i) Its N-terminal sequence has the characteristics of lipoprotein signal sequences, (ii) PemB is synthesised as a high molecular weight precursor processed into a lower molecular weight mature form, (iii) Palmitate, the most prevalent fatty acid in bacterial lipoproteins (12), is incorporated into PemB. [Pg.843]

Although ribosomal proteins are readily observed as in Figures 13.7 and 13.8 altered matrix conditions can alter the relative ionization of bacterial whole-cell compounds. A systematic analysis involving laser power/fluence and sample preparation conditions reveals that if the concentrated trifluo-roacetic acid is added and the laser power increased above optimal conditions, ionization of bacterial surface compounds can be enhanced. Figure 13.9 is the resulting 9.4 T MALDI-FTMS, seen are both the Braun s lipoprotein56,57 and the Murein lipoprotein. Both of these compounds are complex combinations of hydrocarbon lipids attached to a protein base. This is the first MALDI-FTMS observation of surface proteins desorbed directly from whole cells by influencing ionization conditions. [Pg.291]

New insights into the analysis of hydrophobically post-translational modified proteins could be achieved by the construction of lipidated proteins in a combination of bioorganic synthesis of activated lipopeptides and bacterial expression of the protein backbone (Fig. 19). The physico-chemical properties of such artificial lipoproteins differ substantially from those of the corresponding lipopeptides. The pronounced dominance of the hydrophilic protein moiety (e.g., for the Ras protein 181 amino acids) over a short lipopeptide with one or two hydrophobic modifications provides solubility up to 10 4 mol/1, while the biotinylated or fluorescence labeled lipopeptides exhibit low solubility in aqueous solutions and can be applied in the biophysical experiments only in vesicle integrated form or dissolved in organic solvent. [Pg.107]

Bacterial lipoproteins are anchored at the membrane by their covalently linked lipid moiety. Although they are first anchored at the inner membrane on their synthesis, some portion of them are then transfered to the outer membrane. Therefore, some sorting machinery must exist. It has been revealed that there is a specific pathway that includes the... [Pg.297]

Klein, P., Somorjai, R., and Lau, P. (1988). Distinctive properties of signal sequences from bacterial lipoproteins. Protein Eng. 2, 15—20. [Pg.337]

A lipoprotein present in the periplasmic space of E. coli is anchored to the outer bacterial membrane by a triacylated modified N-terminal cysteine containing a glyceryl group in thioether linkage as shown in the following structure (see also Section E,l). [Pg.402]

O-antigen of 180 structures of 430 Lipoprotein(s) 58 bacterial 428 Liposomes 392, 392-394 NMR spectra 396 Liquid crystals 392-394 Liquid crystalline phases 392 Lithium salts, in treatment of manic-depressive illness 564 Lithostatine 443 Liverworts 29... [Pg.922]

Phospholipid molecules in the plasma membrane diffuse rapidly enough to go from one end of an average-sized animal cell to the other in a few minutes. In a bacterial cell, such a trip would take only a few seconds. Integral membrane proteins move more slowly than phospholipids, as we expect in view of their greater mass. Diffusion of membrane proteins plays essential roles in many biochemical processes, including the cellular uptake of lipoproteins (chapter 18), responses of cells to hormones (chapter 24), immunological reactions (supplement 3), vision (supplement 2), and the transport of nutrients and ions. As we see in a later section, however, some membrane proteins cannot move about rapidly because they are attached to cytoskeletal scaffolds. [Pg.393]

Shimizu, T., Ohtsuka, Y., Yanagihara, Y., Kurimura, M., Takemoto, M., and Achiwa, K. (1991) Comparison of biologic activities of synthetic lipopentapeptide analogs of bacterial lipoprotein in mice. Mol. Biother. 3(1), 46-50. [Pg.262]

Bacterial lipoproteins (LP) are structural components of bacterial cell walls consisting of an S-glycerylcysteine moiety, where the glyceryl moiety is di-O-acylated and the cysteine residue is conjugated to the amino-terminus of various polypeptides. In addition, the cysteine a-amine may be acylated with an... [Pg.208]


See other pages where Bacterial lipoproteins is mentioned: [Pg.98]    [Pg.414]    [Pg.98]    [Pg.414]    [Pg.932]    [Pg.1239]    [Pg.178]    [Pg.837]    [Pg.839]    [Pg.390]    [Pg.221]    [Pg.316]    [Pg.379]    [Pg.6]    [Pg.421]    [Pg.280]    [Pg.344]    [Pg.136]    [Pg.184]    [Pg.317]    [Pg.378]    [Pg.119]    [Pg.564]    [Pg.202]    [Pg.1186]    [Pg.1249]    [Pg.218]    [Pg.195]    [Pg.213]    [Pg.432]    [Pg.436]    [Pg.206]    [Pg.184]    [Pg.508]    [Pg.208]    [Pg.216]   
See also in sourсe #XX -- [ Pg.428 ]

See also in sourсe #XX -- [ Pg.428 ]

See also in sourсe #XX -- [ Pg.428 ]

See also in sourсe #XX -- [ Pg.428 ]




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Bacterial membranes lipoprotein

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