Periplasmically-exported lupanine hydroxylase undergoes transition from soluble to functional inclusion bodies in Escherichia coli

Archives of Biochemistry and Biophysics

Volumn 484, Issue 1, 2009, Pages 8-15

  Stampolidis, Pavlos ^a   Kaderbhai, Naheed N ^a   Kaderbhai, Mustak A ^a  

^a ABERYSTWYTH UNIVERSITY   (United Kingdom)

Author keywords

Amorphous protein aggregation; Disulphide bond formation; Inclusion bodies; LH; Periplasmic space; Post translational modifications; Protein export; Pyrroloquinoline quinine; Quinocytochrome c

Indexed keywords

CYTOCHROME C; HEME; HEMOPROTEIN; LUPANIN HYDROXYLASE; LUPANINE; OXYGENASE; QUINOCYTOCHROME C; UNCLASSIFIED DRUG;

ARTICLE; CALCIUM BINDING; CELL INCLUSION; CYTOPLASM; DISULFIDE BOND; ENZYME SYNTHESIS; ESCHERICHIA COLI; HYDROXYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN PROCESSING; SIGNAL TRANSDUCTION; SOLID; SOLUBILITY; TEMPERATURE DEPENDENCE;

BASE SEQUENCE; DISULFIDES; DNA PRIMERS; ENZYME ACTIVATION; ESCHERICHIA COLI; INCLUSION BODIES; MICROSCOPY, ELECTRON; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PERIPLASM; PROTEIN TRANSPORT; RECOMBINANT PROTEINS; SOLUBILITY;

ESCHERICHIA COLI; PSEUDOMONAS;

EID: 62349139780     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.01.017     Document Type: Article

References (63)

1. Ventura S., and Villaverde A. Trends Biotechnol. 24 (2006) 179-185
2. Maier T., Ferbitz L., Deuerling E., and Ban N. Curr. Opin. Struct. Biol. 15 (2005) 204-212
3. Xu Z., and Sigler P.B. J. Struct. Biol. 124 (1998) 129-141
4. Martinez-Alonso M., Vera A., and Villaverde A. FEMS Microbiol. Lett. 273 (2007) 187-195
5. Gonzalez-Montalban N., Natalello A., Garcia-Fruitos E., Villaverde A., and Doglia S.M. Biotechnol. Bioeng. 100 (2008) 797-802
6. Sklar J.G., Wu T., Kahne D., and Silhavy T.J. Genes Dev. 21 (2007) 2473-2484
7. Gonzalez-Montalban N., Garcia-Fruitos E., Ventura S., Aris A., and Villaverde A. Microb. Cell Fact. 5 (2006) 26
8. Villaverde A., and Carrio M.M. Biotechnol. Lett. 25 (2003) 1385-1395
9. Minton A.P. J. Biol. Chem. 276 (2001) 10577-10580
10. Rinas U., and Bailey J.E. Appl. Environ. Microbiol. 59 (1993) 561-566
11. Sorensen H.P., Kristensen J.E., Sperling-Petersen H.U., and Mortensen K.K. Biochem. Biophys. Res. Commun. 319 (2004) 715-719
12. Rajan R.S., Illing M.E., Bence N.F., and Kopito R.R. Proc. Natl. Acad. Sci. USA 98 (2001) 13060-13065
13. Bowden G.A., Paredes A.M., and Georgiou G. Biotechnology (NY) 9 (1991) 725-730
14. Schumann W., and Ferreira L.C.S. Genet. Mol. Biol. 27 (2004) 442-453
15. Weibezahn J., Bukau B., and Mogk A. Microb. Cell Factories 3 (2004) 1
16. Singh S.M., and Panda A.K. J Biosci. Bioeng. (2005) 303-310
17. de Groot N.S., and Ventura S. J. Biotechnol. 125 (2006) 110-113
18. Garcia-Fruitos E., Aris A., and Villaverde A. Appl. Environ. Microbiol. 73 (2007) 289-294
19. Gonzalez-Montalban N., Garcia-Fruitos E., and Villaverde A. Nat. Biotechnol. 25 (2007) 718-720
20. Arie J.P., Miot M., Sassoon N., and Betton J.M. Mol. Microbiol. 62 (2006) 427-437
21. Cayley D.S., Guttman H.J., and Record Jr. M.T. Biophys. J. 78 (2000) 1748-1764
22. Koch A.L. Crit. Rev. Microbiol. 24 (1998) 23-59
23. Kaderbhai N.N., Harding V., and Kaderbhai M.A. Mol. Memb. Biol. 25 (2008)
24. Regeimbal J., and Bardwell J.C.A. In: Dalbey R.E., and von Heijne G. (Eds). Protein Target. Transport Translocat. (2002), Academic Press, Amsterdam 131-150
25. Kaderbhai M.A., Hopper D.J., Akhtar K.M., Abbas S.K., and Kaderbhai N.N. Appl. Environ. Microbiol 69 (2003) 4727-4731
26. Hopper D.J., Kaderbhai M.A., Marriott S.A., Young M., and Rogozinski J. Biochem. J. 367 (2002) 483-489
27. Pan K.L., Hsiao H.C., Weng C.L., Wu M.S., and Chou C.P. J. Bacteriol. 185 (2003) 3020-3030
28. Peng S.B., Wang L., Moomaw J., Peery R.B., Sun P.M., Johnson R.B., Lu J., Treadway P., Skatrud P.L., and Wang Q.M. J. Bacteriol. 183 (2001) 621-627
29. Hunke S., and Betton J.M. Mol. Microbiol. 50 (2003) 1579-1589
30. Kaderbhai M.A., Davey H.M., and Kaderbhai N.N. Protein Sci. 13 (2004) 2458-2469
31. Liu Y., Fu X., Shen J., Zhang H., Hong W., and Chang Z. Biochem. Biophys. Res. Commun. 316 (2004) 795-801
32. Schlapschy M., Grimm S., and Skerra A. Protein Eng. Des. Sel. 19 (2006) 385-390
33. Georgiou G., Telford J.N., Shuler M.L., and Wilson D.B. Appl. Environ. Microbiol. 52 (1986) 1157-1161
34. Miot M., and Betton J.M. Microb. Cell Fact. 3 (2004) 4
35. Tsumoto K., Ejima D., Kumagai I., and Arakawa T. Protein Expr. Purif. 28 (2003) 1-8
36. Hopper D.J., Rogozinski J., and Toczko M. Biochem. J. 279 (1991) 105-109
37. Karim A., Kaderbhai N., Evans A., Harding V., and Kaderbhai M.A. Biotechnology (NY) 11 (1993) 612-617
38. Bradford M. Anal. Biochem. 72 (1976) 248-254
39. Gallagher J., Kaderbhai N., and Kaderbhai M.A. Appl. Microbiol. Biotechnol. 38 (1992) 77-83
40. Goodhew C.F., Wilson I.B., Hunter D.J., and Pettigrew G.W. Biochem. J. 271 (1990) 707-712
41. van Gelder B.F., and Slater E.C. Biochim. Biophys. Acta 58 (1962) 593-595
42. Stevenson C.L., and Hageman M.J. Pharm. Res. 12 (1995) 1671-1676
43. Roberts I.M. J. Microsc. 207 (2002) 97-107
44. Reynolds E.S. J. Biol. Chem. 17 (1963) 208-215
45. Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. Int. J. Neural. Syst. 8 (1997) 581-599
46. Thony-Meyer L. Biochem. Soc. Trans. 30 (2002) 633-638
47. Thony-Meyer L. Microbiol. Mol. Biol. Rev. 61 (1997) 337-376
48. Hopper D.J., and Kaderbhai M.A. Biochim. Biophys. Acta 1647 (2003) 110-115
49. Anthony C. Biochem. J. 320 (1996) 697-711
50. Riener C.K., Kada G., and Gruber H.J. Anal. Bioanal. Chem. 373 (2002) 266-276
51. Wang L., Zhou Q., Chen H., Chu Z., Lu J., Zhang Y., and Yang S. J. Ind. Microbiol. Biotechnol. 34 (2007) 187-192
52. Asherie N. Methods 34 (2004) 266-272
53. Garcia-Fruitos E., Gonzalez-Montalban N., Morell M., Vera A., Ferraz R.M., Aris A., Ventura S., and Villaverde A. Microb. Cell Fact. 4 (2005) 27
54. Ignatova Z. Microb. Cell Fact. 4 (2005) 23
55. Brass J.M., Higgins C.F., Foley M., Rugman P.A., Birmingham J., and Garland P.B. J. Bacteriol. 165 (1986) 787-794
56. Hobot J.A., Carlemalm E., Villiger W., and Kellenberger E. J. Bacteriol. 160 (1984) 143-152
57. Ellis R.J. Curr. Opin. Struct. Biol. 11 (2001) 114-119
58. Schnell S., and Turner T.E. Prog. Biophys. Mol. Biol. 85 (2004) 235-260
59. Burg M.B. Cell Physiol. Biochem. 10 (2000) 251-256
60. Baneyx F., and Mujacic M. Nat. Biotechnol. 22 (2004) 1399-1408
61. Stagg L., Zhang S.Q., Cheung M.S., and Wittung-Stafshede P. Proc. Natl. Acad. Sci. USA 104 (2007) 18976-18981
62. Brass J.M., Higgins C.F., Foley M., Rugman P.A., Birmingham J., and Garland P.B. J. Bacteriol. 165 (1986) 787-795
63. Choi J.H., and Lee S.Y. Appl. Microbiol. Biotechnol. 64 (2004) 625-635