Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli

Journal of Biological Chemistry

Volumn 272, Issue 17, 1997, Pages 11236-11243

  Vlamis Gardikas, Alexios ^a   Åslund, Fredrik ^a   Spyrou, Giannis ^a   Bergman, Tomas ^a   Holmgren, Arne ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GLUTATHIONE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; ESCHERICHIA COLI; GENE EXPRESSION; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; REDUCTION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; CLONING, MOLECULAR; ESCHERICHIA COLI; GENES, BACTERIAL; GLUTATHIONE; INSULIN; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN BIOSYNTHESIS; PROTEIN STRUCTURE, SECONDARY; PROTEINS; RECOMBINANT PROTEINS; RESTRICTION MAPPING; SEQUENCE ANALYSIS, DNA; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; FELIS CATUS;

EID: 0030895581     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.17.11236     Document Type: Article

References (44)

1. Holmgren, A. (1985) Annu. Rev. Biochem. 54, 237-271
2. Holmgren, A. (1989) J. Biol. Chem. 264, 13963-13966
3. Holmgren, A., and Åslund, F. (1995) Methods Enzymol. 252, 283-292
4. Holmgren, A. (1976) Proc. Natl. Acad. Sci. U. S. A. 73, 2275-2279
5. Holmgren, A. (1979) J. Biol. Chem. 254, 3664-3671
6. Åslund, F., Ehn, B., Miranda-Vizuete, A., Pueyo, C., and Holmgren, A. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 9813-9817
7. Åslund, F., Nordstrand, K., Berndt, K. D., Nikkola, M., Bergman, T., Ponstingl, H., Jörnvall, H., Otting, G., and Holmgren, A. (1996) J. Biol. Chem. 271, 6736-6745
8. Sodano, P., Xia, T., Bushweller, J. H., Björnberg, O., Holmgren, A., Billeter, M., and Wüthrich, K. (1991) J. Mol. Biol. 221, 1311-1324
9. Xia, T.-H., Bushweller, J. H., Sodano, P., Billeter, M., Björnberg, O., Holmgren, A., and Wüthrich, K. (1992) Protein Sci. 1, 310-321
10. Holmgren, A., Söderberg, B.-O., Eklund, H., and Bränden, C.-I. (1975) Proc. Natl. Acad. Sci. U. S. A. 72, 2305-2309
11. Martin, J. L. (1995) Structure 3, 245-250
12. Holmgren, A., and Björnstedt, M. (1995) Methods Enzymol. 252, 199-208
13. LaVallie, E. R., DiBlasio, E. A., Kovacic, S., Grant, K. L., Schendel, P. F., and McCoy, J. M. (1993) Bio / technology 11, 187-193
14. Bradford, M. M. (1976) Anal. Biochem. 141, 515-522
15. Bergman, T., and Jörnvall, H. (1987) Eur. J. Biochem. 169, 9-12
16. Kohara, Y., Akiyama, K., and Isono, K. (1987) Cell 50, 495-508
17. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1987) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
18. Collet, T. A., Roben, P., O'Kennedy, R., Barbas, C. F., III, Burton, D. R., and Lerner, R. A. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 10026-10030
19. Laemmli, U. K. (1970) Nature 227, 680-685
20. Bäckström, D., Sjöberg, R.-M., and Lundberg, L. G. (1986) Eur. J. Biochem. 160, 77-82
21. White-Ziegler, C. A., and Low, D. A. (1992) J. Bacteriol. 174, 7003-7012
22. Persson, B., and Argos, P. (1994) J. Mol. Biol. 237, 182-192
23. Alldread, R. M., Nicholls, D. J., Sundaram, T. K., Scawen, M. D., and Atkinson, T. (1992) Gene 114, 139-143
24. Padilla, C. A., Martinez-Galisteo, E., Bárcena, T., Spyrou, G., and Holmgren, A. (1995) Eur. J. Biochem. 227, 27-34
25. Padilla, C. A., Spyrou, G., and Holmgren, A. (1996) FEBS Lett. 378, 69-73
26. Derman, A. I., Prinz, W. A., Belin, D., and Beckwith, J. (1993) Science 262, 1744-1747
27. Bushweller, J. N., Billeter, M., Holmgren, A., and Wüthrich, K. (1994) J. Mol. Biol. 235, 1585-1597
28. Ji, X., von Rosenvinge, E. C., Johnson, W. W., Tomarev, S. I., Piatigorsky, J., Armstrong, R. N., and Gilliland, G. L. (1995) Biochemistry 34, 5317-5328
29. Rost, B., and Sander, C. (1993) J. Mol. Biol. 232, 584-599
30. Ladenstein, R., Epp. O., Bartels, K., Jones, A., Huber, R., and Wendel, A. (1979) J. Mol. Biol. 134, 199-218
31. Dirr, H., Reinemer, P., and Huber, R. (1994) Eur. J. Biochem. 220, 645-661
32. Ji, X., Zhang, P., Armstrong, R. N., and Gilliland, G. L., (1992) Biochemistry 31, 10169-10184
33. Nishida, M., Kong, K.-H., Inoue, H., and Takahashi, K. (1994) J. Biol. Chem. 269, 32536-32541
34. Martin, J. L., Bardwell, J. C. A., and Kuriyan, J. (1993) Nature 365, 464-468
35. Darby, N. J., and Creighton, T. E. (1995) Biochemistry 34, 11725-11735
36. Chen, W.-J., Graminski, G. F., and Armstrong, R. N. (1988) Biochemistry 27, 647-654
37. Graminski, G. F., Zhang, P., Sesay, M. A., Ammon, H. L., and Armstrong, R. N. (1989) Biochemistry 28, 6252-6258
38. Yamaguchi, A., Someya, Y., and Sawai, T. (1992) J. Biol. Chem. 267, 19155-19162
39. von Heijne, G. (1992) J. Mol. Biol. 225, 487-494
40. Griffith, J. K., Baker, M. E., Rouch, A. D., Page, M. G. P., Skurray, R. A., Paulsen, I. T., Chater, K. F., Baldwin, A., and Henderson, P. J. F. (1992) Curr. Opin. Cell Biol. 4, 684-695
41. Yoshida, H., Bugaki, M., Nakamura, K., Ubukata, K., and Konno, M. (1990) J. Bacteriol. 17, 6942-6949
42. Neyfakh, A. (1992) Antimicrob. Agents Chemother. 36, 484-485
43. Apontoweil, P., and Berends, M. (1975) Biochim. Biophys. Acta 399, 1-9
44. Miranda-Vizuete, A., Rodriguez-Ariza, A., Toribio, F., Holmgren, A., López-Barea, J., and Pueyo, C. (1996) J. Biol. Chem. 271, 19099-19103