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Gene Review

osmB  -  osmotically and stress inducible lipoprotein

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1278, JW1275
 
 
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Disease relevance of osmB

  • Transcription in vitro of two osmoregulated promoters, for the Escherichia coli osmB and osmY genes, was analysed using two species of RNA polymerase holoenzyme reconstituted from purified core enzyme and either sigma D (sigma 70, the major sigma in exponentially growing cells) or sigma S (sigma 38, the principal sigma at stationary growth phase) [1].
  • Inactivation of phage T5 by lysed cells after phage multiplication is prevented by a phage-encoded lipoprotein (Llp) that inactivates the FhuA outer membrane receptor protein (K. Decker, V. Krauel, A. Meesmann, and K. Heller, Mol. Microbiol. 12:321-332, 1994) [2].
  • Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an L-methionine-binding protein [3].
  • The immunodominant 38-kDa lipoprotein antigen of Mycobacterium tuberculosis is a phosphate-binding protein [4].
  • The OprM lipoprotein of Pseudomonas aeruginosa is a member of the MexAB-OprM xenobiotic-antibiotic transporter subunits that is assumed to serve as the drug discharge duct across the outer membrane [5].
 

High impact information on osmB

  • This recognition mechanism provides the basis for regulation of protein transport from the TGN to endosomes/lysosomes, which is shared by sortilin and low-density lipoprotein receptor-related protein [6].
  • Selection of multicopy suppressors of the temperature-sensitive phenotype of cells lacking sigmaE revealed that overexpression of the lipoprotein NlpE restored high temperature growth to these cells [7].
  • Human serum albumin, high density and low density lipoprotein, and IgG together protect erythrocytes and platelets against attack by even high doses (5-25 micrograms/ml) of ECH [8].
  • Spleen cells from these mice were unresponsive to a series of B-cell mitogens including LPS prepared from Escherichia coli K235 and from E. coli 0111:B4, lipoprotein mitogen from E. coli, and Nocardia water-soluble mitogen (NWSM) [9].
  • A complex of structures including the Ig-receptor molecules, the LPS receptor, and the lipoprotein receptor appear involved in the regulation of mitogenic stimulation of B cells to proliferation and differentiation to IgM-secreting cells [10].
 

Chemical compound and disease context of osmB

 

Biological context of osmB

 

Anatomical context of osmB

  • A novel protein that is essential for the release of Lpp from the inner membrane was discovered in the periplasm and purified [20].
  • The major outer membrane lipoprotein (Lpp) expressed in spheroplasts was, however, retained in the inner membrane as a mature form [20].
  • The apo-form of peptidoglycan-anchored major lipoprotein (Lpp) and two other outer membrane lipoproteins accumulated in the plasma membrane when lnt expression was reduced [21].
  • The hybrid genes were preceded by a ribosome binding site (RBS) and were expressed under transcriptional control of both the lipoprotein promoter (Plpp) and the lac promoter-operator (POlac) [22].
  • Anti-immunoglobulin antibodies inhibit the mitogenic stimulation of B cells by lipoprotein [10].
 

Associations of osmB with chemical compounds

  • Although a larger part of the protein was extractable with sodium dodecyl sulfate, a part of the hybrid protein was covalently bound to the peptidoglycan layer as the lipoprotein is [19].
  • Globomycin inhibited maturation of protein D in H. influenzae, implying that protein D is exported through the lipoprotein export pathway [23].
  • The putative mature 341-amino-acid-residue XylF (calculated molecular mass of 37,069 Da) appears to be a lipoprotein attached to the cell membrane via a lipid anchor covalently linked to the N-terminal cysteine, as demonstrated by metabolic labelling of the recombinant XylF with [14C]palmitate [24].
  • EDTA treatment induced losses of LPS (up to 40%), outer membrane proteins OmpA, OmpF/C, and lipoprotein, periplasmic proteins, and phosphatidylethanolamine [12].
  • The recombinant K4(2) did not bind to either lysine- or proline-Sepharose, suggesting that the ligand binding activities of lipoprotein (a) may reside in the other kringle domains of apolipoprotein (a) [25].
 

Regulatory relationships of osmB

  • On the other hand, new inner membrane lipoprotein YafY strongly induced degP expression irrespective of the mode of fusion even though the level of overproduced YafY was lower than that of NlpE [17].
 

Other interactions of osmB

  • Alteration of the lipoprotein-sorting signals of NlpE and YafY did not abolish the degP induction [17].
  • Accordingly, the gene has been named nlpE (for new lipoprotein E) [26].
  • The haemolytic activity of E. coli carrying multiple copies of slyA is found mainly in the cytoplasm, with some in the periplasm of cells grown to stationary phase, but overexpression of SlyB, a 15 kDa lipoprotein probably located in the outer membrane, may lead to enhanced, albeit unspecific, release of the haemolytic activity into the medium [27].
 

Analytical, diagnostic and therapeutic context of osmB

  • By site-directed mutagenesis of the 19Ag lipoprotein leader sequence, we have generated a mutant gene which directs the production of 19Ag into the periplasmic space of E. coli, from where it can be easily purified in high yield [28].
  • In conclusion, a convenient protein engineering strategy for converting non-lipoprotein to lipoprotein for commercial application has been devised and tested successfully [29].
  • Eighteen hours after an intraperitoneal injection of endotoxin, the hepatic LDL-receptor expression and the plasma lipoprotein pattern were analyzed [30].
  • We believe that the molecular cloning and characterization of N-SMase cDNA will accelerate the process to define its role as a key regulator in apoptosis, lipid and lipoprotein metabolism, and other cell regulatory pathways [31].
  • Immunoblotting analysis using the antibody against the 45-kDa protein revealed a 48-kDa precursor of the protein, which accumulated in the cyanobacterial cells treated with globomycin, an antibiotic that specifically inhibits cleavage of the signal peptide of lipoprotein precursors [32].

References

  1. Promoter selectivity control of Escherichia coli RNA polymerase by ionic strength: differential recognition of osmoregulated promoters by E sigma D and E sigma S holoenzymes. Ding, Q., Kusano, S., Villarejo, M., Ishihama, A. Mol. Microbiol. (1995) [Pubmed]
  2. Inactivation of FhuA at the cell surface of Escherichia coli K-12 by a phage T5 lipoprotein at the periplasmic face of the outer membrane. Braun, V., Killmann, H., Herrmann, C. J. Bacteriol. (1994) [Pubmed]
  3. Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an L-methionine-binding protein. Deka, R.K., Neil, L., Hagman, K.E., Machius, M., Tomchick, D.R., Brautigam, C.A., Norgard, M.V. J. Biol. Chem. (2004) [Pubmed]
  4. The immunodominant 38-kDa lipoprotein antigen of Mycobacterium tuberculosis is a phosphate-binding protein. Chang, Z., Choudhary, A., Lathigra, R., Quiocho, F.A. J. Biol. Chem. (1994) [Pubmed]
  5. Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end. Akama, H., Kanemaki, M., Yoshimura, M., Tsukihara, T., Kashiwagi, T., Yoneyama, H., Narita, S., Nakagawa, A., Nakae, T. J. Biol. Chem. (2004) [Pubmed]
  6. Structural basis for recognition of acidic-cluster dileucine sequence by GGA1. Shiba, T., Takatsu, H., Nogi, T., Matsugaki, N., Kawasaki, M., Igarashi, N., Suzuki, M., Kato, R., Earnest, T., Nakayama, K., Wakatsuki, S. Nature (2002) [Pubmed]
  7. The response to extracytoplasmic stress in Escherichia coli is controlled by partially overlapping pathways. Connolly, L., De Las Penas, A., Alba, B.M., Gross, C.A. Genes Dev. (1997) [Pubmed]
  8. Potent leukocidal action of Escherichia coli hemolysin mediated by permeabilization of target cell membranes. Bhakdi, S., Greulich, S., Muhly, M., Eberspächer, B., Becker, H., Thiele, A., Hugo, F. J. Exp. Med. (1989) [Pubmed]
  9. Synergistic genetic defect in B-lymphocyte function. I. Defective responses to B-cell stimulants and their genetic basis. Bona, C., Mond, J.J., Paul, W.E. J. Exp. Med. (1980) [Pubmed]
  10. The lipoprotein of the outer membrane of Escherichia coli: a B-lymphocyte mitogen. Melchers, F., Braun, V., Galanos, C. J. Exp. Med. (1975) [Pubmed]
  11. Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli. Choi, D.S., Yamada, H., Mizuno, T., Mizushima, S. J. Biol. Chem. (1986) [Pubmed]
  12. Release of outer membrane fragments from wild-type Escherichia coli and from several E. coli lipopolysaccharide mutants by EDTA and heat shock treatments. Marvin, H.J., ter Beest, M.B., Witholt, B. J. Bacteriol. (1989) [Pubmed]
  13. Lipoprotein from the osmoregulated ABC transport system OpuA of Bacillus subtilis: purification of the glycine betaine binding protein and characterization of a functional lipidless mutant. Kempf, B., Gade, J., Bremer, E. J. Bacteriol. (1997) [Pubmed]
  14. The Tp38 (TpMglB-2) lipoprotein binds glucose in a manner consistent with receptor function in Treponema pallidum. Deka, R.K., Goldberg, M.S., Hagman, K.E., Norgard, M.V. J. Bacteriol. (2004) [Pubmed]
  15. Molecular characterization of a Campylobacter jejuni lipoprotein with homology to periplasmic siderophore-binding proteins. Park, S.F., Richardson, P.T. J. Bacteriol. (1995) [Pubmed]
  16. Sequence of an osmotically inducible lipoprotein gene. Jung, J.U., Gutierrez, C., Villarejo, M.R. J. Bacteriol. (1989) [Pubmed]
  17. Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm. Miyadai, H., Tanaka-Masuda, K., Matsuyama, S., Tokuda, H. J. Biol. Chem. (2004) [Pubmed]
  18. Roles of the hydrophobic cavity and lid of LolA in the lipoprotein transfer reaction in Escherichia coli. Watanabe, S., Matsuyama, S., Tokuda, H. J. Biol. Chem. (2006) [Pubmed]
  19. Mechanism of localization of major outer membrane lipoprotein in Escherichia coli. Studies with the OmpF-lipoprotein hybrid protein. Yu, F., Furukawa, H., Nakamura, K., Mizushima, S. J. Biol. Chem. (1984) [Pubmed]
  20. A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane. Matsuyama, S., Tajima, T., Tokuda, H. EMBO J. (1995) [Pubmed]
  21. Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. Robichon, C., Vidal-Ingigliardi, D., Pugsley, A.P. J. Biol. Chem. (2005) [Pubmed]
  22. Efficient secretion of biologically active recombinant OB protein (leptin) in Escherichia coli, purification from the periplasm and characterization. Guisez, Y., Faché, I., Campfield, L.A., Smith, F.J., Farid, A., Plaetinck, G., Van der Heyden, J., Tavernier, J., Fiers, W., Burn, P., Devos, R. Protein Expr. Purif. (1998) [Pubmed]
  23. Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae, is a lipoprotein. Janson, H., Hedén, L.O., Forsgren, A. Infect. Immun. (1992) [Pubmed]
  24. The D-xylose-binding protein, XylF, from Thermoanaerobacter ethanolicus 39E: cloning, molecular analysis, and expression of the structural gene. Erbeznik, M., Strobel, H.J., Dawson, K.A., Jones, C.R. J. Bacteriol. (1998) [Pubmed]
  25. Expression and purification of kringle 4-type 2 of human apolipoprotein (a) in Escherichia coli. Li, Z., Gambino, R., Fless, G.M., Copeland, R.A., Halfpenny, A.J., Scanu, A.M. Protein Expr. Purif. (1992) [Pubmed]
  26. Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway. Snyder, W.B., Davis, L.J., Danese, P.N., Cosma, C.L., Silhavy, T.J. J. Bacteriol. (1995) [Pubmed]
  27. SlyA, a regulatory protein from Salmonella typhimurium, induces a haemolytic and pore-forming protein in Escherichia coli. Ludwig, A., Tengel, C., Bauer, S., Bubert, A., Benz, R., Mollenkopf, H.J., Goebel, W. Mol. Gen. Genet. (1995) [Pubmed]
  28. Production of the 19-kDa antigen of Mycobacterium tuberculosis in Escherichia coli and its purification. Prestidge, R.L., Grandison, P.M., Chuk, D.W., Booth, R.J., Watson, J.D. Gene (1995) [Pubmed]
  29. Bacterial lipid modification of proteins for novel protein engineering applications. Kamalakkannan, S., Murugan, V., Jagannadham, M.V., Nagaraj, R., Sankaran, K. Protein Eng. Des. Sel. (2004) [Pubmed]
  30. Endotoxin suppresses mouse hepatic low-density lipoprotein-receptor expression via a pathway independent of the toll-like receptor 4. Liao, W., Rudling, M., Angelin, B. Hepatology (1999) [Pubmed]
  31. Molecular cloning, characterization, and expression of a novel human neutral sphingomyelinase. Chatterjee, S., Han, H., Rollins, S., Cleveland, T. J. Biol. Chem. (1999) [Pubmed]
  32. Substrate-binding lipoprotein of the cyanobacterium Synechococcus sp. strain PCC 7942 involved in the transport of nitrate and nitrite. Maeda, S., Omata, T. J. Biol. Chem. (1997) [Pubmed]
 
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