Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum

Journal of Cell Biology

Volumn 138, Issue 6, 1997, Pages 1229-1238

  Holst, Bjørn ^a   Tachibana, Christine ^a,b   Winther, Jakob R ^a  

^a CARLSBERG LABORATORY   (Denmark)

^b PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE ISOMERASE; DITHIOTHREITOL; ISOMERASE; SERINE CARBOXYPEPTIDASE; UNCLASSIFIED DRUG;

ARTICLE; ENDOPLASMIC RETICULUM; ENZYME ACTIVE SITE; FUNGUS GROWTH; GROWTH RATE; MUTATION; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURE ACTIVITY RELATION; YEAST;

BINDING SITES; DITHIOTHREITOL; ENDOPLASMIC RETICULUM; ESCHERICHIA COLI; FUNGAL PROTEINS; GLYCOSYLATION; ISOMERASES; MUTAGENESIS; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SULFHYDRYL REAGENTS; THIOREDOXIN;

FUNGI;

EID: 0030807389     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.138.6.1229     Document Type: Article

References (45)

1. Bardwell, J.C., and J. Beckwith. 1993. The bonds that tie: catalyzed disulfide bond formation [comment). Cell. 74:769-771.
2. Bardwell, J.C., K. McGovern, and J. Beckwith. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell. 67:581-589.
3. Braakman, I., H. Hoover-Litty, K.R. Wagner, and A. Helenius. 1991. Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol. 114: 401-411.
4. Chivers, P.T., M.C. Laboissiere, and R.T. Raines. 1996. The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. EMBO (Eur. Mol. Biol. Orgin.) J. 15:2659-2667.
5. Creighton, T.E., D.A. Hillson, and R.B. Freedman. 1980. Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulfide bonds. J. Mol. Biol. 142:43-62.
6. Darby, N.J., and T.E. Creighton. 1995a. Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase. Biochemistry. 34:16770-16780.
7. Darby, N.J., and T.E. Creighton. 1995b. Functional properties of the individual thioredoxin-likc domains of protein disulfide isomerase. Biochemistry. 34: 11725-11735.
8. Edman, J.C., L. Ellis, R.W. Blacher, R.A. Roth, and W.J. Rutter. 1985. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature (Lond.). 317:267-270.
9. Farquhar, R., N. Honey, S.J. Murant, P. Bossier, L. Schultz, D. Montgomery, R.W. Ellis, R.B. Freedman, and M.F. Tuile. 1991. Protein disulfide isomerase is essential for viability in Saccharomyces cerevisitie. Gene (Amst.). 108:81-89.
10. Gething, M.-J., K. McCammon, and J. Sambrook. 1986. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell. 46:939-950.
11. Givol, D., F. DeLorenzo, R.F. Goldberger, and C.B. Anfinsen. 1965. Disulfide interchange and the three-dimentional structure of proteins. Proc. Natl. Acad. Sci. USA. 53:676-684.
12. Grauschopf, U., J.R. Winther, P. Korber, T. Zander, P. Dallinger, and J.C. Bardwell. 1995. Why is DsbA such an oxidizing disulfide catalyst? Cell. 83: 947-955.
13. Günther, R., C. Bräuer, B. Janetzky, H.H. Förster, I.M. Ehbrecht, L. Lehle, and H. Küntzel. 1991. The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes a lumenal endoplasmic retiiculum glycoprotein involved in the maturation of vacuolar carhoxypeptidase. J. Biol. Cheni. 266:24557-24563.
14. Herlitze, S., and M. Koenen. 1990. A general and rapid mutagenesis method using polymerase chain reaction. Gene (Amst.). 91:143-147.
15. Holst, B., A.W. Bruun, M.C. Kielland-Brandt, and J.R. Winther. 1996. Competition between folding and glycosylation in the endoplasmic reticulum. EMBO (Eur. Mol. Biol. Orgin.) J. 15:3538-3546.
16. Hwang, C., A.J. Sinskey, and H.F. Lodish. 1992. Oxidized redox state of glulathione in the endoplasmic reticulum. Science (Wash. DC). 257:1496-1502.
17. Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
18. Jämsä, E., M. Simonen, and M. Makarow. 1994. Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent. Yeast. 10:355-370.
19. Kemmink, J., N.J. Darby, K. Dijkstra, M. Nilges, and T.E. Creighton. 1996. Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry. 35:7684-7691.
20. Kramer, B., W. Kramer, and H.-J. Fritz. 1984. Different base/base mismatches are corrected with different efficiencies by the methyl-directed DNA mismatch-repair system in E. coli. Cell. 38:879-887.
21. Kunkel, T.A., J.D. Roberts, and R.A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154: 367-381.
22. Kurjan, J. 1985. Alpha-factor structural gene mutations in Saccharomyces cerevisiae: effects on alpha-factor production and mating. Mol. Cell Biol. 5:787-796.
23. Laboissiere, M.C., S.L. Sturley, and R.T. Raines. 1995. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270:28006-28009.
24. LaMantia. M., T. Miura, H. Tachikawa, H.A. Kaplan, W.J. Lennarz, and T. Mizunaga. 1991. Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast. Proc. Natl. Acad. Sci. USA. 88:4453-4457.
25. LaMantia, M.L., and W.J. Lennarz. 1993. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity [see comments]. Cell. 74:899-908.
26. Lebeche, D., H.A. Lucero, and B. Kaminer. 1994. Calcium binding properties of rabbit liver protein disulfide isomerase. Biochem. Biophys. Res. Commun. 202:556-561.
27. Lewis, M.K., and D.V. Thompson. 1990. Efficient site directed in vitro mutagenesis using ampicillin selection. Nucleic Acids Res. 18:3439-3443.
28. Martin, J.L. 1995. Thioredoxin - a fold for all reasons. Structure. 3:245-250.
29. Olesen, K., and M.C. Kielland-Brandt. 1993. Altering substrate preference of carboxypeptidase Y by a novel strategy of mutagenesis eliminating wild type background. Protein Engin. 6:409-415.
30. Ramos, C., J.R. Winther, and M.C. Kielland-Brandt. 1994. Requirement of the propeptide for in vivo formation of active yeast carboxypeptidase Y. J. Biol. Chem. 269:7006-7012.
31. Sambrook, J., E.F. Fritsch, and T. Maniatis. 1989. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY.
32. Scherens, B., E. Dubois, and F. Messenguy. 1991. Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms. Yeast. 7:185-193.
33. Scherer, S., and R.W. Davis. 1979. Replacement of chromosome segments with altered DNA sequences constructed in vitro. Proc. Natl. Acad. Sci. USA. 76: 4951-4955.
34. Sherman, F. 1991. Getting started with yeast. Methods Enzymol. 194:3-21.
35. Sikorski, R.S., and J.D. Boeke. 1991. In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol. 194:302-318.
36. Sikorski, R.S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
37. Simons, J.F., S. Ferro-Novick, M.D. Rose, and A. Helenius. 1995. BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J. Cell Biol. 130:41-49.
38. Stevens, T.H., B. Esmon, and R. Schekman. 1982. Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole. Cell. 30:439-448.
39. Tachibana, C. and T.H. Stevens. 1992. The yeast EUG1 gene encodes an endoplasmatic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell. Biol. 12:460-4611.
40. Tachikawa, H., Y. Takeuchi, W. Funahashi, T. Miura, X.D. Gao, D. Fujimoto, T. Mizunaga, and K. Onodera. 1995. Isolation and characterization of a yeast gene. MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett. 369:212-216.
41. Walker, K.W., M.M. Lyles, and H.F. Gilbert. 1996. Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine. Biochemistry. 35:1972-1980.
42. Winther, J.R., T.H. Stevens, and M.C. Kielland-Brandt. 1991. Yeast carboxypeptidase Y requires glycosylation for efficient intracellular transport, but not for vacuolar sorting, in vivo stability, or activity. Eur. J. Biochem. 197:681-689.
43. Wunderlich, M., A. Otto, K. Maskos, M. Mucke, R. Seckler, and R. Glockshuber. 1995. Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine. J. Mol. Biol. 247:28-33.
44. Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene (Amst.). 33:103-119.
45. Zell, R., and H.-J. Fritz. 1987. DNA mismatch-repair in Escherichia coli counteracting the hydrolytic deamination of 5-methyl-cytosine residues. EMBO (Eur. Mol. Biol. Orgin.) J. 6:1809-1815.