The Structure of RseB: A Sensor in Periplasmic Stress Response of E. coli

Journal of Molecular Biology

Volumn 372, Issue 4, 2007, Pages 927-941

  Wollmann, Petra ^a   Zeth, Kornelius ^b  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b MAX PLANCK INSTITUTE FOR DEVELOPMENTAL BIOLOGY   (Germany)

Author keywords

lipoprotein binding; periplasmic stress response; RseA; RseB; E regulation

Indexed keywords

PERIPLASMIC PROTEIN; PROTEIN RSEA; PROTEIN RSEB; SIGMA FACTOR; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELLULAR STRESS RESPONSE; CRYSTAL STRUCTURE; CYTOPLASM; ESCHERICHIA COLI; MOLECULAR SENSOR; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 34548394160     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.06.039     Document Type: Article

References (65)

1. Raivio T.L., and Silhavy T.J. Periplasmic stress and ECF sigma factors. Annu. Rev. Microbiol. 55 (2001) 591-624
2. Raivio T.L. Envelope stress responses and Gram-negative bacterial pathogenesis. Mol. Microbiol. 56 (2005) 1119-1128
3. Duguay A.R., and Silhavy T.J. Quality control in the bacterial periplasm. Biochim. Biophys. Acta 1694 (2004) 121-134
4. Raffa R.G., and Raivio T.L. A third envelope stress signal transduction pathway in Escherichia coli. Mol. Microbiol. 45 (2002) 1599-1611
5. Cosma C.L., Danese P.N., Carlson J.H., Silhavy T.J., and Snyder W.B. Mutational activation of the Cpx signal transduction pathway of Escherichia coli suppresses the toxicity conferred by certain envelope-associated stresses. Mol. Microbiol. 18 (1995) 491-505
6. Danese P.N., Snyder W.B., Cosma C.L., Davis L.J., and Silhavy T.J. The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease. DegP. Genes Dev. 9 (1995) 387-398
7. Snyder W.B., Davis L.J., Danese P.N., Cosma C.L., and Silhavy T.J. Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway. J. Bacteriol. 177 (1995) 4216-4223
8. E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-σ factor. Genes Dev. 13 (1999) 2449-2461
9. Waller P.R., and Sauer R.T. Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. Science 271 (1996) 990-993
10. Wilken C., Kitzing K., Kurzbauer R., Ehrmann M., and Clausen T. Crystal structure of the DegS stress sensor: how a PDZ domain recognizes misfolded protein and activates a protease. Cell 117 (2004) 483-494
11. Zeth K. Structural analysis of DegS, a stress sensor of the bacterial periplasm. FEBS Letters 569 (2004) 351-358
12. E, RseA. Genes Dev. 16 (2002) 2147-2155
13. E-dependent extracytoplasmic stress response. Genes Dev. 16 (2002) 2156-2168
14. Dartigalongue C., Loferer H., and Raina S. EcfE, a new essential inner membrane protease: its role in the regulation of heat shock response in Escherichia coli. EMBO J. 20 (2001) 5908-5918
15. E with the cytoplasmic domain of its anti-σ RseA. Mol. Cell 11 (2003) 1067-1078
16. Flynn J.M., Levchenko I., Sauer R.T., and Baker T.A. Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation. Genes Dev. 18 (2004) 2292-2301
17. E regulon identified by a two-plasmid system. FEMS Microbiol. Letters 225 (2003) 1-7
18. E stress response in related genomes. PloS Biol. 4 (2006) 43-59
19. E regulon. J. Biol. Chem. 276 (2001) 20866-20875
20. Alba B.M., and Gross C.A. Regulation of the Escherichia coli σ-dependent envelope stress response. Mol. Microbiol. 52 (2004) 613-619
21. E (σ 24) heat shock sigma factor of Escherichia coli. EMBO J. 14 (1995) 1043-1055
22. E subunit of Escherichia coli RNA polymerase: a second alternate σ factor involved in high-temperature gene expression. Genes Dev. 3 (1989) 1462-1471
23. Lipinska B., Sharma S., and Georgopoulos C. Sequence analysis and regulation of the htrA gene of Escherichia coli: a σ 32-independent mechanism of heat-inducible transcription. Nucl. Acids Res. 16 (1988) 10053-10067
24. E regulon. J. Bacteriol. 187 (2005) 4552-4561
25. E, an Escherichia coli heat-inducible σ-factor, is modulated by expression of outer membrane proteins. Genes Dev. 7 (1993) 2618-2628
26. Walsh N.P., Alba B.M., Bose B., Gross C.A., and Sauer R.T. OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell 113 (2003) 61-71
27. E. Mol. Microbiol. 24 (1997) 373-385
28. Cezairliyan B.O., and Sauer R.T. Inhibition of regulated proteolysis by RseB. Proc. Natl Acad. Sci. USA 104 (2007) 3771-3776
29. E envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA. Genes Dev. 18 (2004) 2686-2697
30. E·RNA polymerase. J. Biol. Chem. 275 (2000) 33898-33904
31. E (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins. Mol. Microbiol. 24 (1997) 355-371
32. Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
33. Wollmann P., and Zeth K. Expression, crystallization and preliminary X-ray analysis of the periplasmic stress sensory protein RseB from Escherichia coli. Acta Crystallog. sect. F 62 (2006) 895-898
34. Holm L., and Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20 (1995) 478-480
35. Xu Q., Krishna S.S., McMullan D., Schwarzenbacher R., Miller M.D., Abdubek P., et al. Crystal structure of an ORFan protein (TM1622) from Thermotoga maritima at 1.75 Å resolution reveals a fold similar to the Ran-binding protein Mog1p. Proteins: Struct. Funct. Genet. 65 (2006) 777-782
36. Subbarao G.V., and van den Berg B. Crystal structure of the monomeric porin OmpG. J. Mol. Biol. 360 (2006) 750-759
37. Yildiz O., Vinothkumar K.R., Goswami P., and Kuhlbrandt W. Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation. EMBO J. 25 (2006) 3702-3713
38. Ye J., and van den Berg B. Crystal structure of the bacterial nucleoside transporter Tsx. EMBO J. 23 (2004) 3187-3195
39. Sulzenbacher G., Canaan S., Bordat Y., Neyrolles O., Stadthagen G., Roig-Zamboni V., et al. LppX is a lipoprotein required for the translocation of phthiocerol dimycocerosates to the surface of Mycobacterium tuberculosis. EMBO J. 25 (2006) 1436-1444
40. Camacho L.R., Constant P., Raynaud C., Laneelle M.A., Triccas J.A., Gicquel B., et al. Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier. J. Biol. Chem. 276 (2001) 19845-19854
41. Daffe M., and Laneelle M.A. Distribution of phthiocerol diester, phenolic mycosides and related compounds in mycobacteria. J. Gen. Microbiol. 134 (1988) 2049-2055
42. Matsuyama S., Tajima T., and Tokuda H. A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane. EMBO J. 14 (1995) 3365-3372
43. Matsuyama S., Yokota N., and Tokuda H. A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli. EMBO J. 16 (1997) 6947-6955
44. Tokuda H., and Matsuyama S. Sorting of lipoproteins to the outer membrane in E. coli. Biochim. Biophys. Acta 1693 (2004) 5-13
45. Narita S., Matsuyama S., and Tokuda H. Lipoprotein trafficking in Escherichia coli. Arch. Microbiol. 182 (2004) 1-6
46. Takeda K., Miyatake H., Yokota N., Matsuyama S., Tokuda H., and Miki K. Crystal structures of bacterial lipoprotein localization factors, LolA and LolB. EMBO J. 22 (2003) 3199-3209
47. Taniguchi N., Matsuyama S., and Tokuda H. Mechanisms underlying energy-independent transfer of lipoproteins from LolA to LolB, which have similar unclosed β-barrel structures. J. Biol. Chem. 280 (2005) 34481-34488
48. Watanabe S., Matsuyama S., and Tokuda H. Roles of the hydrophobic cavity and lid of LolA in the lipoprotein transfer reaction in Escherichia coli. J. Biol. Chem. 281 (2006) 3335-3342
49. Dugave C., and Demange L. Cis-trans isomerization of organic molecules and biomolecules: implications and applications. Chem. Rev. 103 (2003) 2475-2532
50. Brandts J.F., Halvorson H.R., and Brennan M. Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14 (1975) 4953-4963
51. Lummis S.C. Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel. Nature 438 (2005) 248-252
52. Braun V., and Rehn K. Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure. Eur. J. Biochem. 10 (1969) 426-438
53. Yakushi T., Tajima T., Matsuyama S., and Tokuda H. Lethality of the covalent linkage between mislocalized major outer membrane lipoprotein and the peptidoglycan of Escherichia coli. J. Bacteriol. 179 (1997) 2857-2862
54. E regulon: role in down-regulation of outer membrane proteins. J. Mol. Biol. 364 (2006) 1-8
55. E-dependent response of Escherichia coli. Mol. Microbiol. 55 (2005) 1403-1412
56. Terwilliger T.C., and Berendzen J. Automated MAD and MIR structure solution. Acta Crystallog. sect. D 55 (1999) 849-861
57. Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallog. sect. D 56 (2000) 965-972
58. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
59. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
60. Vagin A.A., and Teplyakov A. MOLREP: an automated program suite. J. Appl. Crystallog. 30 (1997) 1022-1025
61. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
62. Lee B., and Richards M. The interpretation of proteins structures: Estimation of static accessibility. J. Mol. Biol. 55 (1971) 370-400
63. Claude J.B., Suhre K., Notredame C., Claverie J.M., and Abergel C. CaspR: a web server for automated molecular replacement using homology modelling. Nucl. Acids Res. 32 (2004) W606-W609
64. Thompson J.D., Higginson J., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
65. Diederichs K., and Karplus P.A. Improved R-factors for diffraction data analysis in macromolecular crystallography. Nature Struct. Biol. 4 (1997) 269-275