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Contribution of proteomics toward solving the fascinating mysteries of the biogenesis of the envelope of Escherichia coli

  1. Ruiz, Nat. Rev. Microbiol., 4, 57 (2006)
  2. Tokuda, Biosci. Biotechnol. Biochem., 73, 465 (2009)
  3. Doerrler, Mol. Microbiol., 60, 542 (2006)
  4. Van Wielink, Trends Biochem. Sci., 15, 136 (1990)
  5. Brass J M, Higgins C F, Foley M, Rugman P A, Birmingham J, Garland P B, Lateral diffusion of proteins in the periplasm of Escherichia coli., 10.1128/jb.165.3.787-795.1986
  6. Ehrmann, The Periplasm (2006)
  7. Vollmer, J. Bacteriol., 186, 5978 (2004)
  8. Vollmer, Curr. Opin. Microbiol., 4, 625 (2001)
  9. Weiner, Biochim. Biophys. Acta, 1778, 1698 (2008)
  10. Kol, J. Biol. Chem., 283, 31269 (2008)
  11. Luirink, Annu. Rev. Microbiol., 59, 329 (2005)
  12. Misra, Nucleic Acids Res., 33, D329 (2005)
  13. Baars, J. Bacteriol., 190, 3505 (2008)
  14. Lopez-Campistrous, Mol. Cell. Proteomics, 4, 1205 (2005)
  15. Spelbrink, J. Biol. Chem., 280, 28742 (2005)
  16. Zhang, Proteomics, 7, 484 (2007)
  17. Rabilloud, Electrophoresis, 30, S174 (2009)
  18. Santoni, Electrophoresis, 21, 1054 (2000)
  19. Daley, Science, 308, 1321 (2005)
  20. Natale, Biochim. Biophys. Acta, 1778, 1735 (2008)
  21. Baars, J. Biol. Chem., 281, 10024 (2006)
  22. Wild, Genes Dev., 6, 1165 (1992)
  23. Wild J, Rossmeissl P, Walter W A, Gross C A, Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli., 10.1128/jb.178.12.3608-3613.1996
  24. Sargent, Biochem. Soc. Trans., 35, 835 (2007)
  25. Tullman-Ercek, J. Biol. Chem., 282, 8309 (2007)
  26. Dalbey, Mol. Microbiol., 5, 2855 (1991)
  27. Fountoulakis, Amino Acids, 24, 19 (2003)
  28. Gevaert, Mol. Cell. Proteomics, 1, 896 (2002)
  29. Molloy, Eur. J. Biochem., 267, 2871 (2000)
  30. Riley, Nucleic Acids Res., 34, 1 (2006)
  31. Vertommen, Mol. Microbiol., 67, 336 (2008)
  32. Vertommen, Proteomics, 9, 2432 (2009)
  33. Bardwell, Cell, 67, 581 (1991)
  34. Ito, Curr. Opin. Struct. Biol., 18, 450 (2008)
  35. Messens, Int. J. Biochem. Cell. Biol., 38, 1050 (2006)
  36. Kishigami, FEBS Lett., 364, 55 (1995)
  37. Zapun, Biochemistry, 32, 5083 (1993)
  38. Moutiez Mireille, Quéméneur Eric, Burova Tatiana V., Haertlé Thomas, On the non-respect of the thermodynamic cycle by DsbA variants, 10.1110/ps.8.1.106
  39. Inaba, Biochim. Biophys. Acta, 1783, 520 (2008)
  40. Bardwell, Proc. Natl. Acad. Sci. USA, 90, 1038 (1993)
  41. Bader, Cell, 98, 217 (1999)
  42. Jander, EMBO J., 13, 5121 (1994)
  43. Takahashi, J. Biol. Chem., 279, 47057 (2004)
  44. Guddat, Protein Sci., 6, 1148 (1997)
  45. Dutton, Proc. Natl. Acad. Sci. USA, 105, 11933 (2008)
  46. Kadokura, Science, 303, 534 (2004)
  47. Brennan, J. Biol. Chem., 279, 41352 (2004)
  48. McDonagh, Methods Mol. Biol., 519, 305 (2009)
  49. Hiniker, J. Biol. Chem., 279, 12967 (2004)
  50. Leichert, PLoS Biol., 2, 1723 (2004)
  51. Onder, Mol. Cell. Proteomics, 7, 875 (2008)
  52. Messens, J. Biol. Chem., 282, 31302 (2007)
  53. Stewart, EMBO J., 18, 5963 (1999)
  54. Collet, J. Biol. Chem., 277, 26886 (2002)
  55. Katzen, Cell, 103, 769 (2000)
  56. Rietsch A, Bessette P, Georgiou G, Beckwith J, Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin., 10.1128/jb.179.21.6602-6608.1997
  57. Fabianek, J. Bacteriol., 180, 1947 (1998)
  58. Bessette, J. Biol. Chem., 274, 7784 (1999)
  59. Depuydt, Science, 326, 1109 (2009)
  60. Berkmen, J. Biol. Chem., 280, 11387 (2005)
  61. Gothel, Cell. Mol. Life Sci., 55, 423 (1999)
  62. Liu, Proc. Natl. Acad. Sci. USA, 87, 4028 (1990)
  63. Horne, Arch. Microbiol., 163, 357 (1995)
  64. Dartigalongue, EMBO J., 17, 3968 (1998)
  65. Rouviere, Genes Dev., 10, 3170 (1996)
  66. Arie, Mol. Microbiol., 39, 199 (2001)
  67. Justice, J. Bacteriol., 187, 7680 (2005)
  68. Voulhoux, Science, 299, 262 (2003)
  69. Werner, Mol. Microbiol., 57, 1450 (2005)
  70. Wu, Cell, 121, 235 (2005)
  71. Knowles, Nat. Rev. Microbiol., 7, 206 (2009)
  72. Bos, Annu. Rev. Microbiol., 61, 191 (2007)
  73. Tormo A, Almirón M, Kolter R, surA, an Escherichia coli gene essential for survival in stationary phase., 10.1128/jb.172.8.4339-4347.1990
  74. Missiakas, Mol. Microbiol., 21, 871 (1996)
  75. Alba, Mol. Microbiol., 52, 613 (2004)
  76. Ades, Curr. Opin. Microbiol., 11, 535 (2008)
  77. Behrens, EMBO J., 20, 285 (2001)
  78. Bitto, Structure, 10, 1489 (2002)
  79. Lazar S W, Kolter R, SurA assists the folding of Escherichia coli outer membrane proteins., 10.1128/jb.178.6.1770-1773.1996
  80. Onufryk, J. Bacteriol., 187, 4552 (2005)
  81. Sklar, Genes Dev., 21, 2473 (2007)
  82. Bitto, J. Biol. Chem., 278, 49316 (2003)
  83. Walton, Proc. Natl. Acad. Sci. USA, 106, 1772 (2009)
  84. Walton, Mol. Cell, 15, 367 (2004)
  85. Chen, Mol. Microbiol., 19, 1287 (1996)
  86. Harms, J. Biol. Chem., 276, 18804 (2001)
  87. Qu, J. Mol. Biol., 374, 91 (2007)
  88. Schafer, J. Biol. Chem., 274, 24567 (1999)
  89. Bulieris, J. Biol. Chem., 278, 9092 (2003)
  90. Jarchow, Proteomics, 8, 4987 (2008)
  91. Kwon Soon-Bok, Jung Yun-A, Lim Dong-Bin, Proteomic analysis of heat-stable proteins in Escherichia coli, 10.5483/bmbrep.2008.41.2.108
  92. Zhang, Biotechniques, 35, 1032 (2003)
  93. Hullmann, Mol. Microbiol., 69, 926 (2008)
  94. Saul, J. Mol. Biol., 335, 595 (2004)
  95. Lipinska B, Zylicz M, Georgopoulos C, The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase., 10.1128/jb.172.4.1791-1797.1990
  96. Strauch K L, Johnson K, Beckwith J, Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature., 10.1128/jb.171.5.2689-2696.1989
  97. Kadokura, J. Gen. Appl. Microbiol., 47, 133 (2001)
  98. Jones, J. Bacteriol., 184, 5762 (2002)
  99. Cavard D, Lazdunski C, Howard S P, The acylated precursor form of the colicin A lysis protein is a natural substrate of the DegP protease., 10.1128/jb.171.11.6316-6322.1989
  100. Skorko-Glonek, Arch. Biochem. Biophys., 464, 80 (2007)
  101. Krojer, Nature, 453, 885 (2008)
  102. Isaac, Proc. Natl. Acad. Sci. USA, 102, 17775 (2005)
  103. Krojer, Nature, 416, 455 (2002)
  104. Jiang, Proc. Natl. Acad. Sci. USA, 105, 11939 (2008)
  105. Brokx, J. Bacteriol., 186, 3254 (2004)
  106. Miyadai, J. Biol. Chem., 279, 39807 (2004)
  107. Tokuda, Biochim. Biophys. Acta, 1693, 5 (2004)
  108. Okuda, Proc. Natl. Acad. Sci. USA, 106, 5877 (2009)
  109. Yakushi, Nat. Cell Biol., 2, 212 (2000)
  110. Takeda, EMBO J., 22, 3199 (2003)
  111. Watanabe, Protein Sci., 16, 2741 (2007)
  112. Watanabe, J. Biol. Chem., 283, 25421 (2008)
  113. Thanassi, Methods, 20, 111 (2000)
  114. Proft, Cell Mol. Life Sci., 66, 613 (2009)
  115. Choudhury, Science, 285, 1061 (1999)
  116. Sauer, Science, 285, 1058 (1999)
  117. Sauer, Cell, 111, 543 (2002)
  118. Rizzitello, J. Bacteriol., 183, 6794 (2001)
  119. Mogensen, Mol. Microbiol., 57, 326 (2005)
  120. Skorko-Glonek, Acta Biochim. Pol., 53, 585 (2006)
Bibliographic reference Leverrier, Pauline ; Vertommen, Didier ; Collet, Jean-François. Contribution of proteomics toward solving the fascinating mysteries of the biogenesis of the envelope of Escherichia coli. In: Proteomics, Vol. 10, no. 4, p. 771-784 (2010)
Permanent URL http://hdl.handle.net/2078.1/28820