Domains b′ and a′ of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase: The N-terminal domains a and b enhance this function and can be substituted in part by those of ERp57

Journal of Biological Chemistry

Volumn 276, Issue 14, 2001, Pages 11287-11293

  Pirneskoski, Annamari ^a   Ruddock, Lloyd W ^a,b   Klappa, Peter ^b   Freedman, Robert B ^b   Kivirikko, Kari I ^a   Koivunen, Peppi ^a  

^a UNIVERSITY OF OULU   (Finland)

^b UNIVERSITY OF KENT   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CELLS; CROSSLINKING; POLYPEPTIDES; PROTEINS;

ENZYME ACTIVITY;

BIOCHEMISTRY;

PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEIN DISULFIDE ISOMERASE; SOMATOSTATIN; HEAT SHOCK PROTEIN; ISOENZYME; ISOMERASE; PDIA3 PROTEIN, HUMAN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYST; ENZYME ACTIVITY; MICROSOME; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; ANIMAL; CELL LINE; CHEMISTRY; ENZYME ACTIVATION; HUMAN; METABOLISM;

ANIMALIA; INSECTA;

ANIMALS; CELL LINE; ENZYME ACTIVATION; HEAT-SHOCK PROTEINS; HUMANS; ISOENZYMES; ISOMERASES; PROCOLLAGEN-PROLINE DIOXYGENASE; PROTEIN DISULFIDE-ISOMERASE;

EID: 0035815678     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M010656200     Document Type: Article

References (38)

1. Freedman, R. B., Hirst, T. R., and Tuite, M. F. (1994) Trends Biochem. Sci. 19, 331-336
2. Freedman, R. B., and Klappa, P. (1999) in Molecular Chaperones and Protein Folding (Bukau, B., ed) pp. 437-459, Harwood Academic Press, London
3. Kemmink, J., Darby, N. J., Dijkstra, K., Nilges, M., and Creighton, T. E. (1997) Curr. Biol. 7, 239-245
4. Freedman, R. B., Gane, P. J., Hawkins, H. C., Hlodan, R., McLaughlin, S. H., and Parry, J. W. (1998) Biol. Chem. Hoppe-Seyler 379, 321-328
5. Dijkstra, K., Karvonen, P., Pirneskoski, A., Koivunen, P., Kivirikko, K. I., Darby, N. J., van Straaten, M., Scheek, R. M., and Kemmink, J. (1999) J. Biomol. NMR 14, 195-196
6. Kemmink, J., Dijkstra, K., Mariani, M., Scheek, R. M., Penka, E., Nilges, M., and Darby, N. J. (1999) J. Biomol. NMR 13, 357-368
7. Pihlajaniemi, T., Helaakoski, T., Tasanen, K., Myllylä, R., Huhtala, M.-L., Koivu, J., and Kivirikko, K. I. (1987) EMBO J. 6, 643-649
8. Kivirikko, K. I., and Myllyharju, J. (1998) Matrix Biol. 16, 357-368
9. Kivirikko, K. I., and Pihlajaniemi, T. (1998) Adv. Enzymol. Relat. Areas Mol. Biol. 72, 325-398
10. Wetterau, J. R., Combs, K. A., Spinner, S. N., and Aggerbeck, L. P. (1990) J. Biol. Chem. 265, 9801-9807
11. Wetterau, J. R., Combs, K. A., McLean, L. R., Spinner, S. N., and Aggerbeck, L. P. (1991) Biochemistry 30, 9728-9735
12. LaMantia, M., and Lennarz, W. J. (1993) Cell 74, 899-908
13. Cai, H., Wang, C.-C., and Tsou, C.-L. (1994) J. Biol. Chem. 269, 24550-24552
14. Otsu, M., Omura, F., Yoshimori, T., and Kikuchi, M. (1994) J. Biol. Chem. 269, 6874-6877
15. Puig, A., and Gilbert, H. F. (1994) J. Biol. Chem. 269, 7764-7771
16. Puig, A., Lyles, M. M., Noiva, R., and Gilbert, H. F. (1994) J. Biol. Chem. 269, 19128-19135
17. Rupp, K., Birnbach, U., Lundström, J., Nguyen, Van, P., and Söling, H.-D. (1994) J. Biol. Chem. 269, 2501-2507
18. Hayano, T., Hirose, M., and Kikuchi, M. (1995) FEBS Lett. 377, 505-511
19. Klappa, P., Hawkins, H. C., and Freedman, R. B. (1997) Eur. J. Biochem. 248, 37-42
20. Yao, Y., Zhou, Y.-C., and Wang, C.-C. (1997) EMBO J. 16, 651-658
21. Prockop, D. J., and Kivirikko, K. I. (1995) Annu. Rev. Biochem. 64, 403-434
22. Vuori, K., Pihlajaniemi, T., Marttila, M., and Kivirikko, K. I. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 7467-7470
23. John, D. C. A., Grant, M. E., and Bulleid, N. J. (1993) EMBO J. 12, 1587-1592
24. Lamberg, A., Jauhiainen, M., Metso, J., Enholm, C., Shoulders, C., Scott, J., Pihlajaniemi, T., and Kivirikko, K. I. (1996) Biochem. J. 315, 533-536
25. Vuori, K., Pihlajaniemi, T., Myllylä, R., and Kivirikko, K. I. (1992) EMBO J. 11, 4213-4217
26. Klappa, P., Ruddock, L. W., Darby, N. J., and Freedman, R. B. (1998) EMBO J. 17, 927-935
27. Darby, N. J., Penka, E., and Vincentelli, R. (1998) J. Mol. Biol. 276, 239-247
28. Klappa, P., Koivunen, P., Pirneskoski, A., Karvonen, P., Ruddock, L. W., Kivirikko, K. I., and Freedman, R. B. (2000) J. Biol. Chem. 275, 13213-13218
29. Koivunen, P., Pirneskoski, A., Karvonen, P., Ljung, J., Helaakoski, T., Notbohm, H., and Kivirikko, K. I. (1999) EMBO J. 18, 65-74
30. Oliver, J. D., van der Wal, F. J., Bulleid, N. J., and High, S. (1997) Science 275, 86-88
31. Oliver, J. D., Roderick, H. L., Llewellyn, D. H., and High, S. (1999) Mol. Biol. Cell 10, 2573-2582
32. Koivunen, P., Helaakoski, T., Annunen, P., Veijola, J., Räisänen, S., Pihlajaniemi, T., and Kivirikko, K. I. (1996) Biochem. J. 316, 599-605
33. Helaakoski, T., Annunen, P., Vuori, K., MacNeil, I. A., Pihlajaniemi, T., and Kivirikko, K. I. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 4427-4431
34. Annunen, P., Helaakoski, T., Myllyharju, J., Veijola, J., Pihlajaniemi, T., and Kivirikko, K. I. (1997) J. Biol. Chem. 272, 17342-17348
35. Gruenwald, S., and Heitz, J. (1994) Baculovirus Expression Vector System, Procedures and Methods Manual, Pharmingen, San Diego, CA
36. Kivirikko, K. I., and Myllylä, R. (1982) Methods Enzymol. 82, 245-304
37. Klappa, P., Mayinger, P., Pipkorn, R., Zimmermann, M., and Zimmermann, R. (1991) EMBO J. 10, 2795-2803
38. Myllyharju, J., and Kivirikko, K. I. (1999) EMBO J. 18, 306-312