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Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria

Bibliographic reference Van Laer, Koen ; Buts, Lieven ; Foloppe, Nicolas ; Vertommen, Didier ; Van Belle, Karolien ; et. al. Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria. In: Molecular Microbiology, Vol. 86, no. 00, p. 787-804 (2012)
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  1. Alphey Magnus S., Leonard Gordon A., Gourley David G., Tetaud Emmanuel, Fairlamb Alan H., Hunter William N., The High Resolution Crystal Structure of RecombinantCrithidia fasciculataTryparedoxin-I, 10.1074/jbc.274.36.25613
  2. Antelmann Haike, Helmann John D., Thiol-Based Redox Switches and Gene Regulation, 10.1089/ars.2010.3400
  3. Åslund Fredrik, Berndt Kurt D., Holmgren Arne, Redox Potentials of Glutaredoxins and Other Thiol-Disulfide Oxidoreductases of the Thioredoxin Superfamily Determined by Direct Protein-Protein Redox Equilibria, 10.1074/jbc.272.49.30780
  4. Brünger A. T., Adams P. D., Clore G. M., DeLano W. L., Gros P., Grosse-Kunstleve R. W., Jiang J. S., Kuszewski J., Nilges M., Pannu N. S., Read R. J., Rice L. M., Simonson T., Warren G. L., Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination, 10.1107/s0907444998003254
  5. Bryk R., Metabolic Enzymes of Mycobacteria Linked to Antioxidant Defense by a Thioredoxin-Like Protein, 10.1126/science.1067798
  6. Buchmeier Nancy, Fahey Robert C., ThemshAgene encoding the glycosyltransferase of mycothiol biosynthesis is essential inMycobacterium tuberculosisErdman, 10.1111/j.1574-6968.2006.00441.x
  7. Buchmeier N. A., Newton G. L., Fahey R. C., A Mycothiol Synthase Mutant of Mycobacterium tuberculosis Has an Altered Thiol-Disulfide Content and Limited Tolerance to Stress, 10.1128/jb.00393-06
  8. Bulaj Grzegorz, Kortemme Tanja, Goldenberg David P., Ionization−Reactivity Relationships for Cysteine Thiols in Polypeptides†, 10.1021/bi973101r
  9. Bushweller John H., Aaslund Fredrik, Wuethrich Kurt, Holmgren Arne, Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14.fwdarw.S) and its mixed disulfide with glutathione, 10.1021/bi00153a023
  10. Chai Y.C., Ashraf S.S., Rokutan K., Johnston R.B., Thomas J.A., S-Thiolation of Individual Human Neutrophil Proteins Including Actin by Stimulation of the Respiratory Burst: Evidence against a Role for Glutathione Disulfide, 10.1006/abbi.1994.1167
  11. Chi Bui Khanh, Gronau Katrin, Mäder Ulrike, Hessling Bernd, Becher Dörte, Antelmann Haike, S-Bacillithiolation Protects Against Hypochlorite Stress inBacillus subtilisas Revealed by Transcriptomics and Redox Proteomics, 10.1074/mcp.m111.009506
  12. Collet Jean-Francois, Messens Joris, Structure, Function, and Mechanism of Thioredoxin Proteins, 10.1089/ars.2010.3114
  13. Collinson E. J., Wheeler G. L., Garrido E. O., Avery A. M., Avery S. V., Grant C. M., The Yeast Glutaredoxins Are Active as Glutathione Peroxidases, 10.1074/jbc.m111686200
  14. Delaglio Frank, Grzesiek Stephan, Vuister GeertenW., Zhu Guang, Pfeifer John, Bax Ad, NMRPipe: A multidimensional spectral processing system based on UNIX pipes, 10.1007/bf00197809
  15. Dyson H. Jane, Tennant Linda L., Holmgren Arne, Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional proton NMR, 10.1021/bi00231a023
  16. Ehrt Sabine, Schnappinger Dirk, Mycobacterial survival strategies in the phagosome: defence against host stresses, 10.1111/j.1462-5822.2009.01335.x
  17. Eklund, EMBO J, 3, 1443 (1984)
  18. Fernandes Aristi Potamitou, Holmgren Arne, Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System, 10.1089/152308604771978354
  19. Foloppe, Structure, 12, 289 (2004)
  20. Foloppe Nicolas, Nilsson Lennart, Stabilization of the Catalytic Thiolate in a Mammalian Glutaredoxin: Structure, Dynamics and Electrostatics of Reduced Pig Glutaredoxin and its Mutants, 10.1016/j.jmb.2007.05.101
  21. Foloppe Nicolas, Sagemark Johan, Nordstrand Kerstin, Berndt Kurt D., Nilsson Lennart, Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins, 10.1006/jmbi.2001.4767
  22. Gallogly Molly M., Starke David W., Mieyal John J., Mechanistic and Kinetic Details of Catalysis of Thiol-Disulfide Exchange by Glutaredoxins and Potential Mechanisms of Regulation, 10.1089/ars.2008.2291
  23. Gleason Florence K., Mutation of conserved residues inEscherichia colithioredoxin: Effects on stability and function, 10.1002/pro.5560010507
  24. Goldberg Daniel E., Siliciano Robert F., Jacobs William R., Outwitting Evolution: Fighting Drug-Resistant TB, Malaria, and HIV, 10.1016/j.cell.2012.02.021
  25. Güntert P., Mumenthaler C., Wüthrich K., Torsion angle dynamics for NMR structure calculation with the new program Dyana, 10.1006/jmbi.1997.1284
  26. Hansen Rosa E., Østergaard Henrik, Winther Jakob R., Increasing the Reactivity of an Artificial Dithiol−Disulfide Pair through Modification of the Electrostatic Milieu, 10.1021/bi0500372
  27. Heras Begoña, Kurz Mareike, Jarrott Russell, Shouldice Stephen R., Frei Patrick, Robin Gautier, Čemažar Maša, Thöny-Meyer Linda, Glockshuber Rudi, Martin Jennifer L., Staphylococcus aureusDsbA Does Not Have a Destabilizing Disulfide : A NEW PARADIGM FOR BACTERIAL OXIDATIVE FOLDING, 10.1074/jbc.m707838200
  28. Herrmann Torsten, Güntert Peter, Wüthrich Kurt, 10.1023/a:1021614115432
  29. Holmgren A., Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione., 10.1073/pnas.73.7.2275
  30. Holmgren, J Biol Chem, 254, 3664 (1979)
  31. Holmgren A., Soderberg B. O., Eklund H., Branden C. I., Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution., 10.1073/pnas.72.6.2305
  32. JACKETT P. S., ABER V. R., LOWRIE D. B., Virulence of Mycobacterium tuberculosis and Susceptibility to Peroxidative Killing Systems, 10.1099/00221287-107-2-273
  33. Jensen Kristine Steen, Hansen Rosa E., Winther Jakob R., Kinetic and Thermodynamic Aspects of Cellular Thiol–Disulfide Redox Regulation, 10.1089/ars.2008.2297
  34. Jensen Kristine Steen, Winther Jakob R., Teilum Kaare, Millisecond Dynamics in Glutaredoxin during Catalytic Turnover Is Dependent on Substrate Binding and Absent in the Resting States, 10.1021/ja1096539
  35. Johnson, Methods Mol Biol, 278, 313 (2004)
  36. Kallis, J Biol Chem, 255, 10261 (1980)
  37. Kim Min-Sik, Dufour Yann S., Yoo Ji Sun, Cho Yoo-Bok, Park Joo-Hong, Nam Gi-Baeg, Kim Hae Min, Lee Kang-Lok, Donohue Timothy J., Roe Jung-Hye, Conservation of thiol-oxidative stress responses regulated by SigR orthologues in actinomycetes : Conserved thiol-oxidative stress in actinomycetes, 10.1111/j.1365-2958.2012.08115.x
  38. Kortemme Tanja, Creighton Thomas E., Ionisation of Cysteine Residues at the Termini of Model α-Helical Peptides. Relevance to Unusual Thiol pKaValues in Proteins of the Thioredoxin Family, 10.1006/jmbi.1995.0592
  39. Lee J.-W., Soonsanga S., Helmann J. D., A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR, 10.1073/pnas.0702081104
  40. Lennon B. W., Twists in Catalysis: Alternating Conformations of Escherichia coli Thioredoxin Reductase, 10.1126/science.289.5482.1190
  41. Li Min, Yang Qing, Zhang Lianwen, Li Han,, Cui Yunluan, Wu Qingyu, Identification of novel targets of cyanobacterial glutaredoxin, 10.1016/
  42. 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
  43. Li Yuqing, He Zheng-Guo, The Mycobacterial LysR-Type Regulator OxyS Responds to Oxidative Stress and Negatively Regulates Expression of the Catalase-Peroxidase Gene, 10.1371/journal.pone.0030186
  44. Lillig Christopher Horst, Berndt Carsten, Holmgren Arne, Glutaredoxin systems, 10.1016/j.bbagen.2008.06.003
  45. Manca, Infect Immun, 67, 74 (1999)
  46. Martin Jennifer L, Thioredoxin —a fold for all reasons, 10.1016/s0969-2126(01)00154-x
  47. Martin Jennifer L., Bardwell James C. A., Kuriyan John, Crystal structure of the DsbA protein required for disulphide bond formation in vivo, 10.1038/365464a0
  48. Mieyal John J., Gallogly Molly M., Qanungo Suparna, Sabens Elizabeth A., Shelton Melissa D., Molecular Mechanisms and Clinical Implications of Reversible ProteinS-Glutathionylation, 10.1089/ars.2008.2089
  49. 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
  50. Nederveen Aart J., Doreleijers Jurgen F., Vranken Wim, Miller Zachary, Spronk Chris A.E.M., Nabuurs Sander B., Güntert Peter, Livny Miron, Markley John L., Nilges Michael, Ulrich Eldon L., Kaptein Robert, Bonvin Alexandre M.J.J., RECOORD: A recalculated coordinate database of 500+ proteins from the PDB using restraints from the BioMagResBank, 10.1002/prot.20408
  51. Newton G L, Arnold K, Price M S, Sherrill C, Delcardayre S B, Aharonowitz Y, Cohen G, Davies J, Fahey R C, Davis C, Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes., 10.1128/jb.178.7.1990-1995.1996
  52. Newton Gerald L., Bewley Carole A., Dwyer Tammy J., Horn Ronda, Aharonowitz Yair, Cohen Gerald, Davies Julian, Faulkner D. John, Fahey Robert C., The Structure of U17 Isolated from Streptomyces clavuligerus and its Properties as an Antioxidant Thiol, 10.1111/j.1432-1033.1995.0821h.x
  53. Newton G. L., Buchmeier N., Fahey R. C., Biosynthesis and Functions of Mycothiol, the Unique Protective Thiol of Actinobacteria, 10.1128/mmbr.00008-08
  54. Newton G. L., Koledin T., Gorovitz B., Rawat M., Fahey R. C., Av-Gay Y., The Glycosyltransferase Gene Encoding the Enzyme Catalyzing the First Step of Mycothiol Biosynthesis (mshA), 10.1128/jb.185.11.3476-3479.2003
  55. Newton Gerald L., Unson Mia D., Anderberg Sara J., Aguilera Joseph A., Oh Nancy N., delCardayre Stephen B., Av-Gay Yossef, Fahey Robert C., Characterization ofMycobacterium smegmatisMutants Defective in 1-d-myo-Inosityl-2-amino-2-deoxy-α-d-glucopyranoside and Mycothiol Biosynthesis, 10.1006/bbrc.1999.0156
  56. Nordstrand Kerstin, Åslund Fredrik, Holmgren Arne, Otting Gottfried, Berndt Kurt D, NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism 1 1Edited by P. E. Wright, 10.1006/jmbi.1998.2444
  57. 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
  58. Patel Mehul P., Blanchard John S., Expression, Purification, and Characterization ofMycobacterium tuberculosisMycothione Reductase†, 10.1021/bi991025h
  59. Piddington D. L., Fang F. C., Laessig T., Cooper A. M., Orme I. M., Buchmeier N. A., Cu,Zn Superoxide Dismutase of Mycobacterium tuberculosis Contributes to Survival in Activated Macrophages That Are Generating an Oxidative Burst, 10.1128/iai.69.8.4980-4987.2001
  60. 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
  61. Rokutan, J Immunol, 147, 260 (1991)
  62. Roos, Antioxid Redox Signal (2012)
  63. 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
  64. Roos Goedele, Messens Joris, Protein sulfenic acid formation: From cellular damage to redox regulation, 10.1016/j.freeradbiomed.2011.04.031
  65. Rouhier Nicolas, Villarejo Arsenio, Srivastava Manoj, Gelhaye Eric, Keech Olivier, Droux Michel, Finkemeier Iris, Samuelsson Göran, Dietz Karl Josef, Jacquot Jean-Pierre, Wingsle Gunnar, Identification of Plant Glutaredoxin Targets, 10.1089/ars.2005.7.919
  66. Sattler M, Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients, 10.1016/s0079-6565(98)00025-9
  67. Seres, J Immunol, 156, 1973 (1996)
  68. Shaked Ze'ev, Szajewski Richard P., Whitesides George M., Rates of thiol-disulfide interchange reactions involving proteins and kinetic measurements of thiol pKa values, 10.1021/bi00559a004
  69. Shen Yang, Delaglio Frank, Cornilescu Gabriel, Bax Ad, TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts, 10.1007/s10858-009-9333-z
  70. Shiloh Michael U, DiGiuseppe Champion Patricia A, To catch a killer. What can mycobacterial models teach us about Mycobacterium tuberculosis pathogenesis?, 10.1016/j.mib.2009.11.006
  71. Stehr Matthias, Lindqvist Ylva, NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer, 10.1002/prot.20126
  72. Stehr Matthias, Schneider Gunter, Åslund Fredrik, Holmgren Arne, Lindqvist Ylva, Structural Basis for the Thioredoxin-like Activity Profile of the Glutaredoxin-like NrdH-redoxin fromEscherichia coli, 10.1074/jbc.m105094200
  73. Thurlkill Richard L., Grimsley Gerald R., Scholtz J. Martin, Pace C. Nick, pK values of the ionizable groups of proteins, 10.1110/ps.051840806
  74. Trivedi Abhishek, Singh Nisha, Bhat Shabir Ahmed, Gupta Pawan, Kumar Ashwani, Redox Biology of Tuberculosis Pathogenesis, Advances in Microbial Physiology (2012) ISBN:9780123982643 p.263-324, 10.1016/b978-0-12-398264-3.00004-8
  75. Vilchèze Catherine, Av-Gay Yossef, Attarian Rodgoun, Liu Zhen, Hazbón Manzour H., Colangeli Roberto, Chen Bing, Liu Weijun, Alland David, Sacchettini James C., Jacobs Jr William R., Mycothiol biosynthesis is essential for ethionamide susceptibility inMycobacterium tuberculosis, 10.1111/j.1365-2958.2008.06365.x
  76. Vranken Wim F., Boucher Wayne, Stevens Tim J., Fogh Rasmus H., Pajon Anne, Llinas Miguel, Ulrich Eldon L., Markley John L., Ionides John, Laue Ernest D., The CCPN data model for NMR spectroscopy: Development of a software pipeline, 10.1002/prot.20449
  77. Wolff Simon P., [18] Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides, Methods in Enzymology (1994) ISBN:9780121821340 p.182-189, 10.1016/s0076-6879(94)33021-2
  78. Xia Bin, Vlamis-Gardikas Alexios, Holmgren Arne, Wright Peter E, Dyson H.Jane, Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases, 10.1006/jmbi.2001.4721
  79. Yamazaki Toshio, Forman-Kay Julie D., Kay Lewis E., Two-dimensional NMR experiments for correlating carbon-13.beta. and chemical shifts of aromatic residues in 13C-labeled proteins via scalar couplings, 10.1021/ja00076a099
  80. Zheng M., Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation, 10.1126/science.279.5357.1718
  81. Zorzini Valentina, Haesaerts Sarah, Cheung Ambrose, Loris Remy, van Nuland Nico A. J., 1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase, 10.1007/s12104-010-9290-1