The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

TMANO     N,N-dimethylmethanamine oxide

Synonyms: Triox, TMAO, TMAe, TMA-oxide, AG-D-40837, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of trimethyl-oxido-azanium

 

Psychiatry related information on trimethyl-oxido-azanium

 

High impact information on trimethyl-oxido-azanium

  • The trimethylamine N-oxide (TMAO) reductase of Escherichia coli is a soluble periplasmic molybdoenzyme [1].
  • The most intriguing observation is that translocation of the TMAO reductase across the cytoplasmic membrane is independent of the SecY, SecE, SecA and SecB proteins [1].
  • These results strongly suggest that the translocation of the molybdoenzyme TMAO reductase into the periplasm uses a mechanism fundamentally different from general protein translocation [1].
  • The export of the TMAO reductase is driven mainly by the proton motive force, whereas sodium azide exhibits a limited effect on the export [1].
  • Expression of the tor operon is positively controlled by the TorS/TorR phosphorelay system in response to TMAO availability and negatively regulated by apocytochrome TorC [7].
 

Chemical compound and disease context of trimethyl-oxido-azanium

 

Biological context of trimethyl-oxido-azanium

  • ApoTorC negative autoregulation and TMAO induction are thus mediated by the same sensor protein [7].
  • TMAO does not act by causing a chemical dephosphorylation of phosphorylated tau, but it acts to overcome the functional deficit caused by phosphorylation [6].
  • This property was exploited in the performance of miniMu replicon-mediated in vivo cloning of the promoter region of gene(s) positively regulated by TMAO [13].
  • The second open reading frame, torA, was identified as the structural gene for TMAO reductase [13].
  • The effect of insulin concentration, agitation, pH, ionic strength, anions, seeding, and addition of 1-anilinonaphthalene-8-sulfonic acid (ANS), urea, TMAO, sucrose, and ThT on the kinetics of fibrillation was investigated [14].
 

Anatomical context of trimethyl-oxido-azanium

  • Addition of the osmolyte trimethylamine-oxide (TMAO) and the ketolide antibiotic telithromycin (HMR3647) to the reconstitution stimulates its efficiency up to 100-fold yielding a substantially improved system for the in vitro analysis of mutant ribosomes [15].
  • The natural osmolyte trimethylamine N-oxide (TMAO) restores the ability of mutant tau to promote microtubule assembly [16].
  • Treatment of pigs with BAL containing hepatocytes resulted in an improvement of survival, the plasma concentrations of choline and TMAO being decreased in three out of five animals [17].
  • Detergent treatments were examined for their efficacy in purifying trimethylamine-N-oxide (TMAO) demethylase activity from fish muscle microsomes [18].
  • Addition of urea (urea/TMAO, 2:1) did not overcome the detrimental effects of TMAO in the mitochondria of either species [19].
 

Associations of trimethyl-oxido-azanium with other chemical compounds

  • We then studied the effects of organic solvent dimethyl sulfoxide (DMSO), cellular osmolytes glycerol, and trimethylamine N-oxide (TMAO) on aggregate formation and cell death [20].
  • The frdR mutant was also derepressed for nitrate control of the trimethylamine-N-oxide reductase and alcohol dehydrogenase enzymes [21].
  • Stopped-flow methods, monitoring intrinsic tyrosine fluorescence and far-UV circular dichroism, have been used to measure folding and unfolding kinetics as a function of guanidinium hydrochloride (GdnHCl) and monomer concentrations, in 0 and 1 M TMAO [22].
  • The concentrations of choline and TMAO increased from the beginning to the end in animals treated with the BAL containing alginate beads without hepatocytes [17].
  • RESULTS: The patient's urinalyses showed an augmented TMA (12.64+/-0.95 mg/l) and TMAO (88.42+/-0.82 mg/l) excretion 6 h after the overload test representing an oxidation capacity of 84.6%, consistent with a heterozygosis condition [23].
 

Gene context of trimethyl-oxido-azanium

  • We confirmed this genetically and biochemically using a strain in which phage MudII 1734 carrying lacZ was inserted into torA, the structural gene for inducible trimethylamine-N-oxide reductase [24].
  • Co-immunoadsorption experiments indicate that in TMAO each of these and the coactivator SRC-1 are found complexed with AF1 [25].
  • The chemical chaperone trimethylamine-N-oxide (TMAO) also reversed the GFP-PDS-mediated ER collapse and vesiculation, suggesting that exposed hydrophobic stretches of misfolded or aggregated GFP-PDS may contribute to ER retention [26].
  • Significantly, the binding of TBP was modulated by induced folding of the TAD with TMAO [27].
  • Surprisingly, TorR autoregulation is TMAO independent and still occurs in a torS mutant [28].
 

Analytical, diagnostic and therapeutic context of trimethyl-oxido-azanium

  • PKA-phosphorylated tau (2.7 mol phosphates/mol) does not promote tubulin assembly as judged by spectrophotometric and atomic force microscopy measurements, unless trimethylamine N-oxide (TMAO), a natural occurring osmolyte, is included in these assays [6].
  • We show here that in buffers containing the natural osmolyte trimethylamine N-oxide (TMAO), recombinant AF1 folds into more a compact structure, as evidenced by altered fluorescence emission, circular dichroism spectra, and ultracentrifugal analysis [25].
  • Ultracentrifugation studies indicate that AF1/tau1 exists as a monomer in aqueous solution and that the presence of TMAO does not lead to oligomerization or aggregation [25].
  • The equilibrium constant of folding (K(fold)) at 37 degrees C for the P protein was determined to be 0.0071 +/- 0.0005 using a two-state folding model to describe the TMAO titration data [29].
  • Levels were significantly increased after reperfusion (control 0.02 +/- 0.03 micromol/mL, TX24 1.13 +/- 0.22, and TX42 1.89 +/- 0.38, P < 0.001), and correlated with cold ischemia time (r= 0.96) and TMAO (r= 0.94) [30].

References

  1. A novel sec-independent periplasmic protein translocation pathway in Escherichia coli. Santini, C.L., Ize, B., Chanal, A., Müller, M., Giordano, G., Wu, L.F. EMBO J. (1998) [Pubmed]
  2. Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species. Dos Santos, J.P., Iobbi-Nivol, C., Couillault, C., Giordano, G., Méjean, V. J. Mol. Biol. (1998) [Pubmed]
  3. Microbial dimethylsulfoxide and trimethylamine-N-oxide respiration. McCrindle, S.L., Kappler, U., McEwan, A.G. Adv. Microb. Physiol. (2005) [Pubmed]
  4. Photopigments in Rhodopseudomonas capsulata cells grown anaerobically in darkness. Madigan, M., Cox, J.C., Gest, H. J. Bacteriol. (1982) [Pubmed]
  5. Inhibition of the electron transport system in Staphylococcus aureus by trimethylamine-N-oxide. Suzuki, S., Kubo, A., Shinano, H., Takama, K. Microbios (1992) [Pubmed]
  6. Phosphorylated tau can promote tubulin assembly. Tseng, H.C., Lu, Q., Henderson, E., Graves, D.J. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  7. An unsuspected autoregulatory pathway involving apocytochrome TorC and sensor TorS in Escherichia coli. Gon, S., Jourlin-Castelli, C., Théraulaz, L., Méjean, V. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  8. The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain. Crooke, H., Cole, J. Mol. Microbiol. (1995) [Pubmed]
  9. Identification of a new gene, molR, essential for utilization of molybdate by Escherichia coli. Lee, J.H., Wendt, J.C., Shanmugam, K.T. J. Bacteriol. (1990) [Pubmed]
  10. Nitrate- and molybdenum-independent signal transduction mutations in narX that alter regulation of anaerobic respiratory genes in Escherichia coli. Kalman, L.V., Gunsalus, R.P. J. Bacteriol. (1990) [Pubmed]
  11. A mouse model to test the in vivo efficacy of chemical chaperones. Bai, C., Biwersi, J., Verkman, A.S., Matthay, M.A. Journal of pharmacological and toxicological methods. (1998) [Pubmed]
  12. Enhancement of Polyunsaturated Fatty Acid Production by Tn5 Transposon in Shewanella baltica. Amiri-Jami, M., Wang, H., Kakuda, Y., Griffiths, M.W. Biotechnol. Lett. (2006) [Pubmed]
  13. TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon. Méjean, V., Iobbi-Nivol, C., Lepelletier, M., Giordano, G., Chippaux, M., Pascal, M.C. Mol. Microbiol. (1994) [Pubmed]
  14. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Nielsen, L., Khurana, R., Coats, A., Frokjaer, S., Brange, J., Vyas, S., Uversky, V.N., Fink, A.L. Biochemistry (2001) [Pubmed]
  15. Osmolytes stimulate the reconstitution of functional 50S ribosomes from in vitro transcripts of Escherichia coli 23S rRNA. Semrad, K., Green, R. RNA (2002) [Pubmed]
  16. The natural osmolyte trimethylamine N-oxide (TMAO) restores the ability of mutant tau to promote microtubule assembly. Smith, M.J., Crowther, R.A., Goedert, M. FEBS Lett. (2000) [Pubmed]
  17. Follow-up by one- and two-dimensional NMR of plasma from pigs with ischemia-induced acute liver failure treated with a bioartificial liver. Tréhout, D., Desille, M., Doan, B.T., Mahler, S., Frémond, B., Mallédant, Y., Campion, J.P., Desbois, J., Beloeil, J.C., de Certaines, J., Clément, B. NMR in biomedicine. (2002) [Pubmed]
  18. Partial purification of trimethylamine-N-oxide (TMAO) demethylase from crude fish muscle microsomes by detergents. Parkin, K.L., Hultin, H.O. J. Biochem. (1986) [Pubmed]
  19. Solute effects on mitochondria from an elasmobranch (Raja erinacea) and a teleost (Pseudopleuronectes americanus). Ballantyne, J.S., Moon, T.W. J. Exp. Zool. (1986) [Pubmed]
  20. Chemical chaperones reduce aggregate formation and cell death caused by the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch. Yoshida, H., Yoshizawa, T., Shibasaki, F., Shoji, S., Kanazawa, I. Neurobiol. Dis. (2002) [Pubmed]
  21. The frdR gene of Escherichia coli globally regulates several operons involved in anaerobic growth in response to nitrate. Kalman, L.V., Gunsalus, R.P. J. Bacteriol. (1988) [Pubmed]
  22. Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosome. Banks, D.D., Gloss, L.M. Protein Sci. (2004) [Pubmed]
  23. Diagnosis of suspected trimethylaminuria by NMR spectroscopy. Podadera, P., Sipahi, A.M., Arêas, J.A., Lanfer-Marquez, U.M. Clin. Chim. Acta (2005) [Pubmed]
  24. The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers. Silvestro, A., Pommier, J., Pascal, M.C., Giordano, G. Biochim. Biophys. Acta (1989) [Pubmed]
  25. The conformation of the glucocorticoid receptor af1/tau1 domain induced by osmolyte binds co-regulatory proteins. Kumar, R., Lee, J.C., Bolen, D.W., Thompson, E.B. J. Biol. Chem. (2001) [Pubmed]
  26. Protein synthesis inhibitors and the chemical chaperone TMAO reverse endoplasmic reticulum perturbation induced by overexpression of the iodide transporter pendrin. Shepshelovich, J., Goldstein-Magal, L., Globerson, A., Yen, P.M., Rotman-Pikielny, P., Hirschberg, K. J. Cell. Sci. (2005) [Pubmed]
  27. Induced alpha-helix structure in the aryl hydrocarbon receptor transactivation domain modulates protein-protein interactions. Watt, K., Jess, T.J., Kelly, S.M., Price, N.C., McEwan, I.J. Biochemistry (2005) [Pubmed]
  28. The TorR high-affinity binding site plays a key role in both torR autoregulation and torCAD operon expression in Escherichia coli. Ansaldi, M., Simon, G., Lepelletier, M., Méjean, V. J. Bacteriol. (2000) [Pubmed]
  29. Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. Henkels, C.H., Kurz, J.C., Fierke, C.A., Oas, T.G. Biochemistry (2001) [Pubmed]
  30. H-NMR-based metabolic signatures of mild and severe ischemia/reperfusion injury in rat kidney transplants. Serkova, N., Fuller, T.F., Klawitter, J., Freise, C.E., Niemann, C.U. Kidney Int. (2005) [Pubmed]
 
WikiGenes - Universities