Functional analysis of human P5, a protein disulfide isomerase homologue

Journal of Biochemistry

Volumn 132, Issue 3, 2002, Pages 451-455

  Kikuchi, Masakazu ^a   Doi, Eisuke ^a,c   Tsujimoto, Ikuo ^a   Horibe, Tomohisa ^a   Tsujimoto, Yoshiyuki ^b  

^a RITSUMEIKAN UNIVERSITY   (Japan)

^b KYOTO PREFECTURAL UNIVERSITY   (Japan)

^c TAKARA BIO INC   (Japan)

Author keywords

Human P5; Molecular chaperone; Protein disulfide isomerase; Thioredoxin motif

Indexed keywords

CHAPERONE; CITRATE SYNTHASE; COMPLEMENTARY DNA; DISULFIDE; GLUTATHIONE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MUTANT PROTEIN; PROTEIN DISULFIDE ISOMERASE; THIOREDOXIN; THIOSULFATE SULFURTRANSFERASE; P5 PROTEIN, MESOCRICETUS AURATUS; PRIMER DNA; PROTEIN;

ARTICLE; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; GENE EXPRESSION; GENE MUTATION; HUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; CHEMISTRY; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN MOTIF; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI;

AMINO ACID MOTIFS; BASE SEQUENCE; CITRATE (SI)-SYNTHASE; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; HUMANS; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; PROTEIN DISULFIDE-ISOMERASE; PROTEINS; THIOSULFATE SULFURTRANSFERASE;

EID: 0036737949     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a003242     Document Type: Article

References (24)

1. Hayano, T. and Kikuchi, M. (1995) Cloning and sequencing of the cDNA encoding human P5. Gene 164, 377-378
2. Hillson, D.A., Lambert, N., and Freedman, R.B. (1984) Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase. Methods Enzymol. 107, 281-294
3. Sidrauski, C., Chapman, R., and Walter, P. (1998) The unfolded protein response: an intracellular signalling pathway with many surprising features. Trends Cell Biol. 8, 245-249
4. Freedman, R.B. (1992) Protein folding in the cell in Protein Folding (Creighton, T.E., ed.) pp. 455-539, W.H. Freeman & Co., New York
5. Freedman, R.B., Hirst, T.R., and Tuite, M.F. (1994) Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19, 331-336
6. Kanai, S., Toh, H., Hayano, T., and Kikuchi, M. (1998) Molecular evolution of the domain structures of protein disulfide isomerase. J. Mol. Evol. 47, 200-210
7. Ferrari, D.M. and Soling, H.-D. (1999) The protein disulphideisomerase family: unraveling a string of folds. Biochem. J. 339, 1-10
8. Vuori, K., Myllylä, R., Pihlajaniemi, T., and Kivirikko, K.I. (1992) Expression and site-directed mutagensis of human protein disulfide isomerase in Escherichia coli. J Biol. Chem. 167, 7211-7214
9. Lyles, M.M. and Gilbert, H.F. (1994) Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains. J. Biol. Chem. 269, 30946-30952
10. Katiyar, S., Till, E.A., and Lennarz, W.J. (2001) Studies on the function of yeast protein disulfide isomerase in renaturation of proteins. Biochim. Biophys. Acta 1548, 47-56
11. Kramer, B., Ferrari, D.M., Klappa, P., Pöhlmann, N., and Söling, H.-D. (2001) Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding. Biochem. J. 357, 83-95
12. Kunkel, T.A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492
13. Lambert, N. and Freedman, R.B. (1983) Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction. Biochem. J. 213, 235-243
14. Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A.L., and Hartl, F.-U. (1991) Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 352, 36-42
15. Shao, F., Bader, W.M., Jakob, U., and Bardwell, J.C.A. (2000) DsbG, a protein disulfide isomerase with chaperone activity. J. Biol. Chem. 275, 13349-13352
16. Cai, H., Wang, C.-C., and Tsou, C.-L. (1994) Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J Biol. Chem. 269, 24550-24552
17. Horibe, T., Nagai, H., Sakakibara, K., Hagiwara, Y., and Kikuchi, M. (2001) Ribostamycin inhibits the chaperone activity of protein disulfide isomerase. Biochem. Biophys. Res. Commun. 289, 967-972
18. Tachikawa, H., Takeuchi, Y., Funahashi, W., Miura, T., Gao, X.D., Fujimoto, D., Mizunaga, T., and Onodera, K. (1995) Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase. FEBS Lett. 369, 212-216
19. Tachikawa, H., Funahashi, W., Takeuchi, Y., Nakanishi, H., Nishihara, R., Kato, S., Gao, X.D., Mizunaga, T., and Fujimoto, D. (1997) Overexpression of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner. Biochem. Biophys. Res. Commun. 239, 710-714
20. Norgaard, P. and Winther, J.R. (2001) Mutation of yeast Eug1p CXXS active sites to CXXC results in dramatic increase in protein disulfide isomerase activity. Biochem. J. 358, 269-274
21. Wunderlich, M., Otto, A., Maskos, K., Mucke, M., Seckler, R., and Glockshuber, R. (1995) Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine. J. Mol. Biol. 247, 28-33
22. Winter, J., Klappa, P., Freedman, R.B., Lilie, H., and Rudolph, R. (2002) Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin. J. Biol. Chem. 277, 310-317
23. Hayano, T., Hirose, M., and Kikuchi, M. (1995) Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell. FEBS Lett. 377, 505-511
24. Klappa, P., Hawkins, H.C., and Freedman, R.B. (1997) Interactions between protein disulfide isomerase and peptides. Eur. J. Biochem. 248, 37-42