Characterization of molten globule PopB in absence and presence of its chaperone PcrH

Protein Journal

Volumn 31, Issue 5, 2012, Pages 401-416

  Dey, Supratim ^a   Basu, Abhishek ^a   Datta, Saumen ^a  

^a INDIAN INSTITUTE OF CHEMICAL BIOLOGY   (India)

Author keywords

ANS binding; Circular dichroism; Fluorescence; Molten globule; Type III secretion system

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; POPB PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL INFECTION; CELL MEMBRANE; CONTROLLED STUDY; FLUORESCENCE; NONHUMAN; OPERON; PH; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE; PSEUDOMONAS AERUGINOSA;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; FLUORESCENCE; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN DENATURATION; PROTEIN INTERACTION MAPPING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS INFECTIONS; TRYPTOPHAN; UREA;

PSEUDOMONAS AERUGINOSA;

EID: 84864643787     PISSN: 15723887     EISSN: 15734943     Source Type: Journal    
DOI: 10.1007/s10930-012-9416-7     Document Type: Article

References (81)

1. Agashe VR, Udgaonkar JB (1995) Biochemistry 34:3286-3299
2. Arai M, Kuwajima K (2000) Adv Protein Chem 53:209-282
3. Basu A, Chatterjee R, Datta S (2012) Protein J 31:93-107
4. Bertagna AM, Barrick D (2004) Proc Natl Acad Sci USA 101: 12514-12519
5. Blocker A, Gounon P, Larquet E, Niebuhr K, Cabiaux V, Parsot C, Sansonetti P (1999) J Cell Biol 147:683-693
6. Buchan DW, Ward SM, Lobley AE, Nugent TC, Bryson K, Jones DT (2010) Nucl Acids Res 38:W563-W568 (http://bioinf.cs.ucl.ac.uk/psipred/)
7. Buttner CR, Sorg I, Cornelis GR, Heinz DW, Niemann HH (2008) J Mol Biol 375:997-1012
8. Buttner D, Bonas U (2002) Trends Microbiol 10:186-192
9. Chenal A, Savarin P, Nizard P, Guillain F, Gillet D, Forge V (2002) J Biol Chem 277:43425-43432
10. Chiron MF, Fryling CM, FitzGerald DJ (1994) J Biol Chem 269:18167-18176
11. Cole C, Barber JD, Barton GJ (2008) Nucleic Acids Res 35:W197-W201 (http://www.compbio.dundee.ac.uk)
12. Coombes BK, Finlay BB (2005) Trends Microbiol 13:92-95
13. Cornelis GR (2006) Nat Rev Microbiol 4:811-825
14. Creighton TE (1997) Trends Biochem Sci 22:6-10
15. Dacheux D, Goure J, Chabert J, Usson Y, Attree I (2001) Mol Microbiol 40:76-85
16. Derewenda U, Mateja A, Devedjiev Y, Routzahn KM, Evdokimov AG, Derewenda ZS, Waugh DS (2004) Structure 12:301-306
17. Dunker AK, Lawson JD, Brown CJ, Williams RM, Romero P, Oh JS, Oldfield CJ, Campen AM, Ratliff CM, Hipps KW, Ausio J, Nissen MS, Reeves R, Kang C, Kissinger CR, Bailey RW, Griswold MD, Chiu W, Garner EC, Obradovic Z (2001) J Mol Graph Model 19:26-59
18. Dyson HJ, Wright PE (2002) Curr Opin Struct Biol 12:54-60
19. Farahbakhsh ZT, Wisnieski BJ (1989) Biochemistry 28:580-585
20. Faudry E, Job V, Dessen A, Attree I, Forge V (2007) FEBS J 274:3601-3610
21. Faudry E, Vernier G, Neumann E, Forge V, Attree I (2006) Biochemistry 45:8117-8123
22. Finck-Barbancon V, Goranson J, Zhu L, Sawa T, Wiener-Kronish JP, Fleisziq SM, Wu C, Mende-Mueller L, Frank DW (1997) Mol Microbiol 25:547-557
23. Fradin C, Satsoura D, Andrews DW (2009) Punching holes in membranes: biomembrane frontiers, handbook of modern biophysics. Humana Press
24. Francis MS, Aili M, Wiklund ML, Wolf-Watz H (2000) Mol Microbiol 38:85-102
25. Frank DW (1997) Mol Microbiol 26:621-629
26. Frederick KK, Marlow MS, Valentine KG, Wand AJ (2007) Nature 448:325-329
27. Gala'n JE, Wolf-Watz H (2006) Nature 444:567-573
28. Goure J, Pastor A, Faudry E, Chabert J, Dessen A, Attree I (2004) Infect Immun 72:4741-4750
29. Hagihara Y, Tan Y, Goto Y (1994) J Mol Biol 237:336-348
30. Hakansson S, Bergman T, Vanooteghem JC, Cornelis G, Wolf- Watz H (1993) Infect Immun 61:71-80
31. Hamada D, Kato T, Ikegami T, Suzuki KN, Hayashi M, Murooka Y, Honda T, Yanagihara I (2005) FEBS J 272:756-768
32. Hamada D, Kidokoro S, Fukada H, Takahashi K, Goto Y (1994) Proc Natl Acad Sci USA 91:10325-10329
33. Hueck CJ (1998) Microbiol Mol Biol Rev 62:379-433
34. Hueck CJ, Hantman MJ, Bajaj V, Johnston C, Lee CA, Miller SI (1995) Mol Microbiol 18:479-490
35. Job V, Matteï PJ, Lemaire D, Attree I, Dessen A (2010) J Biol Chem 285:23224-23232
36. Johnson S, Roversi P, Espina M, Olive A, Deane JE, Birket S, Field T, Picking WD, Blocker AJ, Galyov EE, Picking WL, Lea SM (2007) J Biol Chem 282:4035-4044
37. Kaniga K, Tucker S, Trollinger D, Galan JE (1995) J Bacteriol 177:3965-3971
38. Karplus M, Ichiye T, Pettitt BM (1987) Biophys J 52:1083-1085
39. Kelly SM, Price NC (1997) Biochim Biophys Acta-Protein Struct Mol Enzymol 1338:161-185
40. Laue, TM, Shah BD, Ridgeway TM, Pelletier SL (1992) Sedimentation interpretation. In: Analytical ultracentrifugation in biochemistry and polymer science, Royal Society of Chemistry
41. Lindeberg M, Zakharov SD, Cramer WA (2000) J Mol Biol 295:679-692
42. Lokareddy RK, Lunelli M, Eilers B, Wolter V, Kolbe M (2010) J Biol Chem 285:39965-39975
43. Lunelli M, Lokareddy RK, Zychlinsky A, Kolbe M (2009) Proc Natl Acad Sci USA 106:9661-9666
44. Lyczak JB, Cannon CL, Pier GB (2000) Microbes Infect 2:1051-1060
45. Marmorino JL, Lehti M, Pielak G (1998) J Mol Biol 275:379-388
46. Meiler J, Baker D (2003) Proc Natl Acad Sci USA 100: 12105-12110 (http://www.meilerlab.org/web/)
47. Mota LJ (2006) Trends Microbiol 14:197-200
48. Mueller CA, Broz P, Muller SA, Ringler P, Erne-Brand F, Sorg I, Kuhn M, Engel A, Cornelis GR (2005) Science 310:674-676
49. Muga A, Gonzalez-Manas JM, Lakey JH, Pattus F, Surewicz WK (1993) J Biol Chem 268:1553-1557
50. Myers JK, Nick Pace C, Scholtz JM (1995) Protein Sci 4:2138-2148
51. Neyt C, Cornelis GR (1999) Mol Microbiol 31:143-156
52. Ohgushi M, Wada A (1984) Adv Biophys 18:75-90
53. Parker MW, Feil SC (2005) Prog Biophys Mol Biol 88:91-142
54. Ptitsyn OB (1995) Adv Protein Chem 47:83-229
55. Ptitsyn OB (1995) Trends Biochem Sci 20:376-379
56. Redfield C, Smith RA, Dobson CM (1994) Nature Struct Biol 1:23-29
57. Romano FB, Rossi KC, Savva CG, Holzenburg A, Clerico EM, Heuck AP (2011) Biochemistry 50:7117-7131
58. Sarker MR, Neyt C, Stainier I, Cornelis GR (1998) J Bacteriol 180:1207-1214
59. Sawa T, Yahr TL, Ohara M, Kurahashi K, Gropper MA, Wiener- Kronish JP, Frank DW (1999) Nat Med 5:392-398
60. Schoehn G, Di Guilmi AM, Lemaire D, Attree I, Weissenhorn W, Dessen A (2003) EMBO J 22:4957-4967
61. Schuck P (2000) Biophys J 78:1606-1619
62. Schuck P, Perugini MS, Gonzales NR, Howlett GJ, Schubert D (2002) Biophys J 82:1096-1111
63. Semisotnov GV, Rodionova NA, Razgulyaev OI, Uversky VN, Gripas AF, Gilmanshi RI (1991) Biopolymers 31:119-128
64. Sheshadri S, Lingaraju GM, Varadarajan R (1999) Protein Sci 8:1689-1695
65. Spolar RS, Record MT Jr (1994) Science 263:777-784
66. Stites WE (1997) Chem Revs 97:1233-1250
67. Sturtevant JM (1977) Proc Natl Acad Sci USA 74:2236-2240
68. Sundin C, Wolfgang MC, Lory S, Forsberg A, Frithz-Lindsten E (2002) Microb Pathog 33:265-277
69. Tan YW, Yu HB, Sivaraman J, Leung KY, Mok YK (2009) Protein Sci 18:1724-1734
70. Tran N, Serfis AB, Osiecki JC, Picking WL, Coye L, Davis R, Picking WD (2000) Infect Immun 68:3710-3715
71. Uversky VN (2002) Eur J Biochem 269:2-12
72. Uversky VN (2002) Protein Sci 11:739-756
73. Uversky VN, Gilespie JR, Fink AL (2000) Proteins 41:415- 427
74. Uversky VN, Winter S, Löber G (1996) Biophys Chem 60:79-88
75. Van der Goot FG, Gonzalez-Manas JM, Lakey JH, Pattus F (1991) Nature 354:408-410
76. Venkatesan MM, Buysse JM, Kopecko DJ (1988) Proc Natl Acad Sci USA 85:9317-9321
77. Whitmore L, Wallace BA (2004) Nucleic Acids Res 32:668-673
78. Wright PE, Dyson HJ (1999) J Mol Biol 293:321-331
79. Yahr TL, Vallis AJ, Hancock MK, Barbieri JT, Frank DW (1998) Proc Natl Acad Sci USA 95:13899-13904
80. Yu XJ, McGourty K, Liu M, Unsworth KE, Holden DW (2010) Science 328:1040-1043
81. Zahn R, Plückthun A (1994) J Mol Biol 242:165-174