User menu

Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics

Bibliographic reference Denoncin, Katleen ; Schwalm, Jaclyn ; Vertommen, Didier ; Silhavy, Thomas ; Collet, Jean-François. Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics. In: Proteomics, Vol. 12, no.9, p. 1391-1401 (2012)
Permanent URL
  1. Leverrier, Proteomics, 9, 2432 (2009)
  2. Bos Martine P., Robert Viviane, Tommassen Jan, Biogenesis of the Gram-Negative Bacterial Outer Membrane, 10.1146/annurev.micro.61.080706.093245
  3. Knowles Timothy J., Scott-Tucker Anthony, Overduin Michael, Henderson Ian R., Membrane protein architects: the role of the BAM complex in outer membrane protein assembly, 10.1038/nrmicro2069
  4. Ruiz Natividad, Kahne Daniel, Silhavy Thomas J., Transport of lipopolysaccharide across the cell envelope: the long road of discovery, 10.1038/nrmicro2184
  5. Silhavy T. J., Kahne D., Walker S., The Bacterial Cell Envelope, 10.1101/cshperspect.a000414
  6. TOKUDA Hajime, Biogenesis of Outer Membranes in Gram-Negative Bacteria, 10.1271/bbb.80778
  7. Tokuda Hajime, Matsuyama Shin-ichi, Sorting of lipoproteins to the outer membrane in E. coli, 10.1016/j.bbamcr.2004.02.005
  8. Wu T., McCandlish A. C., Gronenberg L. S., Chng S.-S., Silhavy T. J., Kahne D., Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli, 10.1073/pnas.0604744103
  9. Ruiz Natividad, Falcone Brian, Kahne Daniel, Silhavy Thomas J., Chemical Conditionality, 10.1016/j.cell.2005.02.014
  10. Wu Tao, Malinverni Juliana, Ruiz Natividad, Kim Seokhee, Silhavy Thomas J., Kahne Daniel, Identification of a Multicomponent Complex Required for Outer Membrane Biogenesis in Escherichia coli, 10.1016/j.cell.2005.02.015
  11. Hagan C. L., Kim S., Kahne D., Reconstitution of Outer Membrane Protein Assembly from Purified Components, 10.1126/science.1188919
  12. Silhavy Thomas J., Ruiz Natividad, Kahne Daniel, Advances in understanding bacterial outer-membrane biogenesis, 10.1038/nrmicro1322
  13. Duguay Amy R., Silhavy Thomas J., Quality control in the bacterial periplasm, 10.1016/j.bbamcr.2004.04.012
  14. Depuydt Matthieu, Messens Joris, Collet Jean-Francois, How Proteins Form Disulfide Bonds, 10.1089/ars.2010.3575
  15. Messens Joris, Collet Jean-François, Pathways of disulfide bond formation in Escherichia coli, 10.1016/j.biocel.2005.12.011
  16. Rizzitello A. E., Harper J. R., Silhavy T. J., Genetic Evidence for Parallel Pathways of Chaperone Activity in the Periplasm of Escherichia coli, 10.1128/jb.183.23.6794-6800.2001
  17. Ureta A. R., Endres R. G., Wingreen N. S., Silhavy T. J., Kinetic Analysis of the Assembly of the Outer Membrane Protein LamB in Escherichia coli Mutants Each Lacking a Secretion or Targeting Factor in a Different Cellular Compartment, 10.1128/jb.01103-06
  18. Rouviere P E, Gross C A, SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins., 10.1101/gad.10.24.3170
  19. Lazar, J Bacteriol, 178, 1770 (1996)
  20. Sklar J. G., Wu T., Kahne D., Silhavy T. J., Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli, 10.1101/gad.1581007
  21. Vertommen Didier, Ruiz Natividad, Leverrier Pauline, Silhavy Thomas J., Collet Jean-François, Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics, 10.1002/pmic.200800794
  22. Gogol E. B., Rhodius V. A., Papenfort K., Vogel J., Gross C. A., Small RNAs endow a transcriptional activator with essential repressor functions for single-tier control of a global stress regulon, 10.1073/pnas.1109379108
  23. Thompson K. M., Rhodius V. A., Gottesman S.,  E Regulates and Is Regulated by a Small RNA in Escherichia coli, 10.1128/jb.00020-07
  24. Rhodius Virgil A, Suh Won Chul, Nonaka Gen, West Joyce, Gross Carol A, Conserved and Variable Functions of the σE Stress Response in Related Genomes, 10.1371/journal.pbio.0040002
  25. Korndörfer Ingo P, Dommel Monica K, Skerra Arne, Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture, 10.1038/nsmb828
  26. Jarchow Svenja, Lück Carsten, Görg Angelika, Skerra Arne, Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp, 10.1002/pmic.200800288
  27. Chen Robert, Henning Ulf, Aperiplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins, 10.1111/j.1365-2958.1996.tb02473.x
  28. Bulieris Paula V., Behrens Susanne, Holst Otto, Kleinschmidt Jörg H., Folding and Insertion of the Outer Membrane Protein OmpA Is Assisted by the Chaperone Skp and by Lipopolysaccharide, 10.1074/jbc.m211177200
  29. Schäfer Ute, Beck Konstanze, Müller Matthias, Skp, a Molecular Chaperone of Gram-negative Bacteria, Is Required for the Formation of Soluble Periplasmic Intermediates of Outer Membrane Proteins, 10.1074/jbc.274.35.24567
  30. Volokhina E. B., Grijpstra J., Stork M., Schilders I., Tommassen J., Bos M. P., Role of the Periplasmic Chaperones Skp, SurA, and DegQ in Outer Membrane Protein Biogenesis in Neisseria meningitidis, 10.1128/jb.00532-10
  31. Krojer Tobias, Sawa Justyna, Schäfer Eva, Saibil Helen R., Ehrmann Michael, Clausen Tim, Structural basis for the regulated protease and chaperone function of DegP, 10.1038/nature07004
  32. Jiang J., Zhang X., Chen Y., Wu Y., Zhou Z. H., Chang Z., Sui S.-F., Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins, 10.1073/pnas.0805464105
  33. Spiess Christoph, Beil Alexandra, Ehrmann Michael, A Temperature-Dependent Switch from Chaperone to Protease in a Widely Conserved Heat Shock Protein, 10.1016/s0092-8674(00)80743-6
  34. Tommassen J., Assembly of outer-membrane proteins in bacteria and mitochondria, 10.1099/mic.0.042689-0
  35. Casadaban Malcolm J., Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu, 10.1016/0022-2836(76)90119-4
  36. Silhavy, Experiments with Gene Fusions (1984)
  37. Baba Tomoya, Ara Takeshi, Hasegawa Miki, Takai Yuki, Okumura Yoshiko, Baba Miki, Datsenko Kirill A, Tomita Masaru, Wanner Barry L, Mori Hirotada, Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection, 10.1038/msb4100050
  38. Cherepanov Peter P., Wackernagel Wilfried, Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant, 10.1016/0378-1119(95)00193-a
  39. Button, J. Bacteriol., 180, 6408 (2007)
  40. Nichols, J. Bacteriol., 189, 1523 (1998)
  41. Misra, J. Biol. Chem., 266, 13592 (1991)
  42. Aoki Stephanie K., Malinverni Juliana C., Jacoby Kyle, Thomas Benjamin, Pamma Rupinderjit, Trinh Brooke N., Remers Susan, Webb Julia, Braaten Bruce A., Silhavy Thomas J., Low David A., Contact-dependent growth inhibition requires the essential outer membrane protein BamA (YaeT) as the receptor and the inner membrane transport protein AcrB, 10.1111/j.1365-2958.2008.06404.x
  43. Vertommen, Mol. Microbiol., 67, 336 (2008)
  44. Liu Hongbin, Sadygov Rovshan G., Yates John R., A Model for Random Sampling and Estimation of Relative Protein Abundance in Shotgun Proteomics, 10.1021/ac0498563
  45. Wagner Jennifer K., Heindl Jason E., Gray Andrew N., Jain Sumita, Goldberg Marcia B., Contribution of the Periplasmic Chaperone Skp to Efficient Presentation of the Autotransporter IcsA on the Surface ofShigella flexneri, 10.1128/jb.00989-08
  46. Purdy G. E., Fisher C. R., Payne S. M., IcsA Surface Presentation in Shigella flexneri Requires the Periplasmic Chaperones DegP, Skp, and SurA, 10.1128/jb.00483-07
  47. Ieva R., Tian P., Peterson J. H., Bernstein H. D., Sequential and spatially restricted interactions of assembly factors with an autotransporter   domain, 10.1073/pnas.1103827108
  48. Charlson E. S., Werner J. N., Misra R., Differential Effects of yfgL Mutation on Escherichia coli Outer Membrane Proteins and Lipopolysaccharide, 10.1128/jb.00571-06
  49. Werner John, Misra Rajeev, YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins ofEscherichia coli : YaeT is a general outer membrane protein assembly factor, 10.1111/j.1365-2958.2005.04775.x
  50. Bennion Drew, Charlson Emily S., Coon Eric, Misra Rajeev, Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli : BamA POTRA 1 mutants, 10.1111/j.1365-2958.2010.07280.x
  51. Kim S., Malinverni J. C., Sliz P., Silhavy T. J., Harrison S. C., Kahne D., Structure and Function of an Essential Component of the Outer Membrane Protein Assembly Machine, 10.1126/science.1143993
  52. Quan Shu, Koldewey Philipp, Tapley Tim, Kirsch Nadine, Ruane Karen M, Pfizenmaier Jennifer, Shi Rong, Hofmann Stephan, Foit Linda, Ren Guoping, Jakob Ursula, Xu Zhaohui, Cygler Miroslaw, Bardwell James C A, Genetic selection designed to stabilize proteins uncovers a chaperone called Spy, 10.1038/nsmb.2016