User menu

Accès à distance ? S'identifier sur le proxy UCLouvain

Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from mycobacterium tuberculosis

  1. World Health Organization. (2012) Global Tuberculosis Report
  2. Rawat M., Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis, 10.1099/mic.0.26084-0
  3. Rawat M., Newton G. L., Ko M., Martinez G. J., Fahey R. C., Av-Gay Y., Mycothiol-Deficient Mycobacterium smegmatis Mutants Are Hypersensitive to Alkylating Agents, Free Radicals, and Antibiotics, 10.1128/aac.46.11.3348-3355.2002
  4. Ta P., Buchmeier N., Newton G. L., Rawat M., Fahey R. C., Organic Hydroperoxide Resistance Protein and Ergothioneine Compensate for Loss of Mycothiol in Mycobacterium smegmatis Mutants, 10.1128/jb.01402-10
  5. Jaeger Timo, Budde Heike, Flohé Leopold, Menge Ulrich, Singh Mahavir, Trujillo Madia, Radi Rafael, Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis, 10.1016/j.abb.2003.11.021
  6. Cole S. T., Barrell B. G., Analysis of the Genome ofMycobacterium tuberculosis H37Rv, Genetics and Tuberculosis ISBN:9780470846520 p.160-177, 10.1002/0470846526.ch12
  7. Van Laer Koen, Buts Lieven, Foloppe Nicolas, Vertommen Didier, Van Belle Karolien, Wahni Khadija, Roos Goedele, Nilsson Lennart, Mateos Luis M., Rawat Mamta, van Nuland Nico A. J., Messens Joris, Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria : Mycoredoxin-1 links mycothiol to oxidative stress, 10.1111/mmi.12030
  8. Ordóñez Efrén, Van Belle Karolien, Roos Goedele, De Galan Sandra, Letek Michal, Gil Jose A., Wyns Lode, Mateos Luis M., Messens Joris, Arsenate Reductase, Mycothiol, and Mycoredoxin Concert Thiol/Disulfide Exchange, 10.1074/jbc.m900877200
  9. Chi B. K. Busche T. Laer K. V. Basell K. Becher D. Clermont L. Seibold G. M. Persicke M. Kalinowski J. Messens J. Antelmann H. (2013) Protein S-Mycothiolation Functions as Redox-Switch and Thiol Protection Mechanism in Corynebacterium glutamicum Under Hypochlorite Stress. Antioxid. Redox Signal., In press
  10. Hugo M. Radi R. Trujillo M. (2012) Thiol dependent peroxidases in Mycobacterium tuberculosis in Understanding Tuberculosis: Deciphering the Secret Life of the Bacilli ( Cardona P.-J. , ed.), InTech. pp. 293–316
  11. Soito Laura, Williamson Chris, Knutson Stacy T., Fetrow Jacquelyn S., Poole Leslie B., Nelson Kimberly J., PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family, 10.1093/nar/gkq1060
  12. Oliva M., Theiler G., Zamocky M., Koua D., Margis-Pinheiro M., Passardi F., Dunand C., PeroxiBase: a powerful tool to collect and analyse peroxidase sequences from Viridiplantae, 10.1093/jxb/ern317
  13. Nathan Carl, Taming Tuberculosis: A Challenge for Science and Society, 10.1016/j.chom.2009.02.004
  14. Li Simon, Peterson Neil A., Kim Min-Young, Kim Chang-Yub, Hung Li-Wei, Yu Minmin, Lekin Timothy, Segelke Brent W., Lott J. Shaun, Baker Edward N., Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys Peroxiredoxin, 10.1016/j.jmb.2004.12.046
  15. Hugo Martín, Turell Lucía, Manta Bruno, Botti Horacio, Monteiro Gisele, Netto Luis E. S., Alvarez Beatriz, Radi Rafael, Trujillo Madia, Thiol and Sulfenic Acid Oxidation of AhpE, the One-Cysteine Peroxiredoxin fromMycobacterium tuberculosis: Kinetics, Acidity Constants, and Conformational Dynamics, 10.1021/bi901221s
  16. Reyes Aníbal M., Hugo Martín, Trostchansky Andrés, Capece Luciana, Radi Rafael, Trujillo Madia, Oxidizing substrate specificity of Mycobacterium tuberculosis alkyl hydroperoxide reductase E: kinetics and mechanisms of oxidation and overoxidation, 10.1016/j.freeradbiomed.2011.04.023
  17. Hildebrandt Alfred G., Roots Ivar, Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes, 10.1016/0003-9861(75)90047-8
  18. Schonbaum, J. Biol. Chem, 247, 3353 (1972)
  19. Ellman George L., Tissue sulfhydryl groups, 10.1016/0003-9861(59)90090-6
  20. Riddles Peter W., Blakeley Robert L., Zerner Burt, Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid)—a reexamination, 10.1016/0003-2697(79)90792-9
  21. Pyr Dit Ruys Sébastien, Wang Xuemin, Smith Ewan M., Herinckx Gaëtan, Hussain Nusrat, Rider Mark H., Vertommen Didier, Proud Christopher G., Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase, 10.1042/bj20111530
  22. Choi Seonhwa, Jeong Jaeho, Na Seungjin, Lee Hyo Sun, Kim Hwa-Young, Lee Kong-Joo, Paek Eunok, New Algorithm for the Identification of Intact Disulfide Linkages Based on Fragmentation Characteristics in Tandem Mass Spectra, 10.1021/pr900771r
  23. Alvarez María Noel, Peluffo Gonzalo, Piacenza Lucía, Radi Rafael, Intraphagosomal Peroxynitrite as a Macrophage-derived Cytotoxin against InternalizedTrypanosoma cruzi : CONSEQUENCES FOR OXIDATIVE KILLING AND ROLE OF MICROBIAL PEROXIREDOXINS IN INFECTIVITY, 10.1074/jbc.m110.167247
  24. Mendes Pedro, GEPASI: a software package for modelling the dynamics, steady states and control of biochemical and other systems, 10.1093/bioinformatics/9.5.563
  25. Roos Goedele, Garcia-Pino Abel, Van belle Karolien, Brosens Elke, Wahni Khadija, Vandenbussche Guy, Wyns Lode, Loris Remy, Messens Joris, The Conserved Active Site Proline Determines the Reducing Power of Staphylococcus aureus Thioredoxin, 10.1016/j.jmb.2007.02.045
  26. Piñeyro María Dolores, Arcari Talia, Robello Carlos, Radi Rafael, Trujillo Madia, Tryparedoxin peroxidases from Trypanosoma cruzi: High efficiency in the catalytic elimination of hydrogen peroxide and peroxynitrite, 10.1016/j.abb.2010.12.014
  27. Villadangos Almudena F., Van Belle Karolien, Wahni Khadija, Tamu Dufe Veronica, Freitas Sofia, Nur Haneen, De Galan Sandra, Gil José A., Collet Jean-Francois, Mateos Luis M., Messens Joris, Corynebacterium glutamicum survives arsenic stress with arsenate reductases coupled to two distinct redox mechanisms : Distinct redox-coupled arsenate reductases in a single organism, 10.1111/j.1365-2958.2011.07882.x
  28. Gu Sheng, Chen Jin, Dobos Karen M., Bradbury E. Morton, Belisle John T., Chen Xian, Comprehensive Proteomic Profiling of the Membrane Constituents of aMycobacterium tuberculosisStrain, 10.1074/mcp.m300060-mcp200
  29. Winterbourn Christine C., Metodiewa Diana, Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide, 10.1016/s0891-5849(99)00051-9
  30. Trujillo Madia, Mauri PierLuigi, Benazzi Louise, Comini Marcelo, De Palma Antonella, Flohé Leopold, Radi Rafael, Stehr Matthias, Singh Mahavir, Ursini Fulvio, Jaeger Timo, The Mycobacterial Thioredoxin Peroxidase Can Act as a One-cysteine Peroxiredoxin, 10.1074/jbc.m601008200
  31. Rouhier Nicolas, Gelhaye Eric, Jacquot Jean Pierre, Glutaredoxin-dependent Peroxiredoxin from Poplar : PROTEIN-PROTEIN INTERACTION AND CATALYTIC MECHANISM, 10.1074/jbc.m111489200
  32. Pedrajas José Rafael, Padilla C. Alicia, McDonagh Brian, Bárcena José Antonio, Glutaredoxin Participates in the Reduction of Peroxides by the Mitochondrial 1-CYS Peroxiredoxin inSaccharomyces cerevisiae, 10.1089/ars.2009.2950
  33. Hanschmann Eva-Maria, Lönn Maria Elisabet, Schütte Lena Dorothee, Funke Maria, Godoy José R., Eitner Susanne, Hudemann Christoph, Lillig Christopher Horst, Both Thioredoxin 2 and Glutaredoxin 2 Contribute to the Reduction of the Mitochondrial 2-Cys Peroxiredoxin Prx3, 10.1074/jbc.m110.185827
  34. Fang Ferric C., Antimicrobial reactive oxygen and nitrogen species: concepts and controversies, 10.1038/nrmicro1004
  35. Reeves Stacy A., Parsonage Derek, Nelson Kimberly J., Poole Leslie B., Kinetic and Thermodynamic Features Reveal ThatEscherichia coliBCP Is an Unusually Versatile Peroxiredoxin, 10.1021/bi200935d
  36. Reynolds C. Michael, Meyer Jacques, Poole Leslie B., An NADH-Dependent Bacterial Thioredoxin Reductase-like Protein in Conjunction with a Glutaredoxin Homologue Form a Unique Peroxiredoxin (AhpC) Reducing System inClostridium pasteurianum†, 10.1021/bi011802p
  37. Bryk R., Metabolic Enzymes of Mycobacteria Linked to Antioxidant Defense by a Thioredoxin-Like Protein, 10.1126/science.1067798
  38. Dormeyer Matthias, Reckenfelderbäumer Nina, Lüdemann Heike, Krauth-Siegel R. Luise, Trypanothione-dependent Synthesis of Deoxyribonucleotides byTrypanosoma bruceiRibonucleotide Reductase, 10.1074/jbc.m010352200
  39. Holmgren, J. Biol. Chem, 254, 3672 (1979)
  40. Van Laer Koen, Dziewulska Aleksandra M., Fislage Marcus, Wahni Khadija, Hbeddou Abderahim, Collet Jean-Francois, Versées Wim, Mateos Luis M., Tamu Dufe Veronica, Messens Joris, NrdH-redoxin ofMycobacterium tuberculosisandCorynebacterium glutamicumDimerizes at High Protein Concentration and Exclusively Receives Electrons from Thioredoxin Reductase, 10.1074/jbc.m112.392688
  41. Delaunay Agnès, Pflieger Delphine, Barrault Marie-Bénédicte, Vinh Joelle, Toledano Michel B., A Thiol Peroxidase Is an H2O2 Receptor and Redox-Transducer in Gene Activation, 10.1016/s0092-8674(02)01048-6
  42. Fomenko D. E., Koc A., Agisheva N., Jacobsen M., Kaya A., Malinouski M., Rutherford J. C., Siu K.-L., Jin D.-Y., Winge D. R., Gladyshev V. N., Thiol peroxidases mediate specific genome-wide regulation of gene expression in response to hydrogen peroxide, 10.1073/pnas.1010721108
  43. Azevedo Dulce, Tacnet Frédérique, Delaunay Agnès, Rodrigues-Pousada Claudina, Toledano Michel B, Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling, 10.1016/s0891-5849(03)00434-9
  44. Nathan C., Shiloh M. U., Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens, 10.1073/pnas.97.16.8841
  45. Newton Gerald, Fahey Robert, Mycothiol biochemistry, 10.1007/s00203-002-0469-4
  46. Van Laer Koen, Hamilton Chris J., Messens Joris, Low-Molecular-Weight Thiols in Thiol–Disulfide Exchange, 10.1089/ars.2012.4964
  47. Patel Mehul P., Blanchard John S., Expression, Purification, and Characterization ofMycobacterium tuberculosisMycothione Reductase†, 10.1021/bi991025h
  48. Rawat Mamta, Johnson Chantale, Cadiz Vanessa, Av-Gay Yossef, Comparative analysis of mutants in the mycothiol biosynthesis pathway in Mycobacterium smegmatis, 10.1016/j.bbrc.2007.08.142
Bibliographic reference Hugo, Martín ; Trujillo, Madia ; Radi, Rafael ; Messens, Joris ; Vertommen, Didier ; et. al. Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from mycobacterium tuberculosis. In: Journal of Biological Chemistry, Vol. 289, no. 8, p. 5228-5239 (2014)
Permanent URL http://hdl.handle.net/2078.1/159754