Replacement of domain b of human protein disulfide isomerase-related protein with domain b′ of human protein disulfide isomerase dramatically increases its chaperone activity

FEBS Letters

Volumn 566, Issue 1-3, 2004, Pages 311-315

  Horibe, Tomohisa ^a   Iguchi, Daisuke ^a   Masuoka, Toshio ^a   Gomi, Mitsuhiro ^a   Kimura, Taiji ^a   Kikuchi, Masakazu ^b  

^a RITSUMEIKAN UNIVERSITY   (Japan)

^b Dept Central R and D Laboratory Kobayashi Pharmaceutical Co LTD   (Japan)

Author keywords

ER, endoplasmic reticulum; GSH, glutathione (reduced form); hPDI, human protein disulfide isomerase; hPDIR, human protein disulfide isomerase related protein; SDS PAGE, sodium dodecyl sulfate polyacrylamide gel electorophoresis

Indexed keywords

ALPHA 1 ANTITRYPSIN; CHAPERONE; PEPTIDE; PROTEIN DISULFIDE ISOMERASE;

ARTICLE; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; MUTANT; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ESCHERICHIA COLI; HUMANS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MUTATION; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE;

EID: 2442477583     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.03.103     Document Type: Article

References (29)

1. Freedman R.B. Creighton T.E. Protein Folding. 1992;W.H. Freeman & Co, New York. pp. 455-539
2. Freedman R.B. Trends Biochem. Sci. 9:1984;438-441
3. Freedman R.B. Cell. 57:1989;1069-1072
4. Bulleid N.J., Freedman R.B. Nature. 335:1988;649-651
5. Vuori K., Myllylä R., Pihlajaniemi T., Kivirikko K.I. J. Biol. Chem. 267:1992;7211-7214
6. Pihlajaniemi T., Helaakoski T., Tasanen K., Myllylä R., Huhtala M.-L., Koivu J., Kivirikko K.I. EMBO J. 6:1987;643-649
7. Wetterau J.R., Combs K.A., Spinner S.N., Joiner B.J. J. Biol. Chem. 265:1990;9800-9807
8. Farquhar R., Honey N., Murant S.J., Bossier P., Schultz L., Montgomery D., Ellis R.W., Freedman R.B., Tuite M.F. Gene. 108:1991;81-89
9. Gunther R., Brauer C., Janetzky B., Forster H.-H., Ehbrecht E.-M., Lehle L., Kuntzel H. J. Biol. Chem. 266:1991;24536-24557
10. LaMantia M.L., Miura T., Tachikawa H., Kaplan H.A., Lennarz W.J., Mizunaga T. Proc. Natl. Acad. Sci. USA. 88:1991;4453-4457
11. Horibe T., Nagai H., Sakakibara K., Hagiwara Y., Kikuchi M. Biochem. Biophys. Res. Commun. 289:2001;967-972
12. Horibe T., Nagai H., Matsui H., Hagiwara Y., Kikuchi M. J. Antibiot. 55:2002;528-530
13. Narindrasorasak S., Yao P., Sarkar B. Biochem. Biophys. Res. Commun. 311:2003;405-414
14. Lebeche D., Lucero H.A., Kaminer B. Biochem. Biophys. Res. Commun. 202:1994;556-561
15. Lucero H.A., Kaminer B. J. Biol. Chem. 274:1999;3243-3251
16. Horibe T., Gomi M., Iguchi D., Ito H., Kitamura Y., Masuoka T., Tsujimoto I., Kimura T., Kikuchi M. J. Biol. Chem. 279:2004;4604-4611
17. Ferrari D.M., Soling H.-D. Biochem. J. 339:1999;1-10
18. Kikuchi M., Doi E., Tsujimoto I., Horibe T., Tsujimoto Y. J. Biochem. 132:2002;451-455
19. Laemmli U.K. Nature. 227:1970;680-685
20. Eisenthal R., Danson M.J. Enzyme Assays. 1992;IRL Oxford University Press. pp. 327-329
21. Lambert N., Freedman R.B. Biochem. J. 213:1983;235-243
22. Martin J., Langer T., Boteva R., Schramel A., Horwich A.L., Hartl F.-U. Nature. 352:1991;36-42
23. Kemmink J., Darby N.J., Dijkstra K., Nilges M., Creighton T.E. Curr. Biol. 7:1997;239-245
24. Darby N.J., Kemmink J., Creighton T.E. Biochemistry. 35:1996;10517-10528
25. Kunkel T.A. Proc. Natl. Acad. Sci. USA. 82:1985;488-492
26. Sun X.X., Dai Y., Liu H.P., Chen S.M., Wang C.C. Biochim. Biophys. Acta. 1481:2000;45-54
27. Klappa P., Ruddock L.W., Darby N.J., Freedman R.B. EMBO J. 17:1998;927-935
28. Klappa P., Hawkins H.C., Freedman R.B. Eur. J. Biochem. 248:1997;37-42
29. Pirneskoski A., Klappa P., Lobell M., Williamson R.A., Byrne L., Alanen H.I., Salo K.E., Kivirikko K.I., Freedman R.B., Ruddock L.W. J. Biol. Chem. 279:2004;10374-10381