Impaired secretion of a hydrophobic cutinase by Saccharomyces cerevisiae correlates with an increased association with immunoglobulin heavy-chain binding protein (BiP)

Applied and Environmental Microbiology

Volumn 64, Issue 1, 1998, Pages 316-324

  Sagt, C M J ^a   Muller W H ^a   Boonstra, J ^a   Verkleij, A J ^a   Verrips, C T ^a,b  

^a UTRECHT UNIVERSITY   (Netherlands)

^b UNILEVER RESEARCH VLAARDINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CUTINASE; GLUCOSE REGULATED PROTEIN; MUTANT PROTEIN;

ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME RELEASE; GENE EXPRESSION REGULATION; HYDROPHOBICITY; IMMUNOELECTRON MICROSCOPY; IMMUNOPRECIPITATION; NONHUMAN; PROMOTER REGION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

EID: 0344474668     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.1.316-324.1998     Document Type: Article

References (32)

1. Aridor, M., and W. E. Balch. 1996. Principles of selective transport: coat complexes hold the key. Trends Cell Biol. 6:315-320.
2. Biemans, R., D. Thines, T. Rutgers, M. DeWilde, and T. Cabezon. 1991. The large surface protein of hepatitis B virus is retained in the yeast endoplasmic reticulum and provokes its unique enlargement. DNA Cell Biol. 10:191-200.
3. Blond-Elguindi, S., S. E. Cwirla, W. J. Dower, R. J. Lipshutz, S. R. Sprang, J. F. Sambrook, and M. J. H. Gething. 1993. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75:717-728.
4. Bole, D. G., L. Hendershot, and J. F. Kearney. 1986. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chain in nonsecreting and secreting hybridomas. J. Cell Biol. 102:1558-1566.
5. Egmond, M. R., H. W. T. M. van der Hijden, W. Musters, H. Peters, and C. T. Verrips. 1994. Patent WO 94/14963.
6. Egmond, M. R., H. W. T. M. van der Hijden, W. Musters, H. Peters, and C. T. Verrips. 1994. Patent WO 94/14964.
7. Gething, M. J., K. McCammon, and J. Sambrook. 1986. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding and intracellular transport. Cell 46:939-950.
8. Gething, M. J., and J. Sambrook. 1992. Protein folding in the cell. Nature 355:33-45.
9. Haas, I. G. 1991. BiP - a heat shock protein involved in immunoglobulin chain assembly. Curr. Top. Microbiol. Immunol. 167:71-82.
10. Haas, I. G., and M. Wabl. 1983. Immunoglobulin heavy chain binding protein. Nature 306:387-389.
11. Humbel, B. M., and H. Schwartz. 1989. Freeze-substitution for immunochemistry, p. 115-134. In A. J. Verkleij and J. L. M. Leunissen (ed.), Immuno-gold labelling in cell biology. CRC Press, Inc., Boca Raton, Fla.
12. Hurtley, S. M., D. G. Bole, L. H. Hoover, A. Helenius, and C. S. Copeland. 1989. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell Biol. 108:2117-2126.
13. Kim, P. S., D. Bole, and P. Arvan. 1992. Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperone, BiP. J. Cell Biol. 118:541-549.
14. Kolattukudy, P. E. 1984. Cutinases from fungi and pollen, p. 471-504. In B. Borgstrom and H. Brockman (ed.), Lipases. Elsevier Science, Amsterdam, The Netherlands.
15. Kozutsumi, Y., M. Segal, K. Normington, M. J. Gething, and J. Sambrook. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose regulated proteins. Nature 332:462-464.
16. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
17. Li, X., Y. Wu, D. Zhang, J. W. Gillikin, R. S. Boston, V. R. Franceschi, and T. W. Okita. 1993. Rice prolamine protein body biogenesis: a BiP-mediated process. Science 262:1054-1056.
18. Martinez, C., P. de Geus, M. Lauwereys, G. Matthysens, and C. Cambillau. 1992. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356:615-618.
19. Müller, W. H., T. P. van der Krift, G. Knoll, E. B. Smaal, and A. J. Verkleij. 1991. A preparation method of specimens of the fungus Penicillium chrysogenum for ultrastructural and immuno-electron microscopical studies. J. Microsc. 169:29-41.
20. Normington, K., K. Kohno, Y. Kozutsumi, M. J. Gething, and J. Sambrook. 1989. S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57:1223-1236.
21. Parekh, R., K. Forrester, and D. Wittrup. 1995. Multicopy overexpression of bovine pancreatic trypsin inhibitor saturates the protein folding and secretory capacity of Saccharomyces cerevisiae. Protein Expr. Purif. 6:537-545.
22. Rose, M. D., L. M. Misra, and J. P. Vogel. 1989. Kar2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57:1211-1221.
23. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
24. Sawa, T., T. Imamura, T. Haruta, T. Sasaoka, M. Ishiki, Y. Takata, Y. Takada, H. Morioka, H. Ishihara, I. Usui, and M. Kobayashi. 1996. Hsp70 family molecular chaperones and mutant insulin receptor: differential binding specificities of BiP and Hsp70/Hsc70 determine accumulation or degradation of insulin receptor. Biochem. Biophys. Res. Commun. 218:449-453.
25. Shamu, C. E., and P. Walter. 1996. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signalling from the endoplasmic reticulum to the nucleus. EMBO J. 15:3028-3039.
26. Shuster, J. R. 1991. Gene expression in yeast: protein secretion. Curr. Opin. Biotechnol. 2:685-690.
27. Sierkstra, L. N., J. M. A. Verbakel, and C. T. Verrips. 1992. Analysis of transcription and translation of glycolytic enzymes in glucose limited continuous cultures of S. cerevisiae. J. Gen. Microbiol. 138:2559-2566.
28. Silljé, H. H. W., E. G. ter Schure, A. J. Verkleij, J. Boonstra, and C. T. Verrips. 1996. The Cdc25 protein of Saccharomyces cerevisiae is required for normal glucose transport. Microbiology 142:1765-1773.
29. Sitte, H., K. Neumann, and L. Edelmann. 1985. Cryofixation and cryosubstitution for routine work in transmission electron microscopy, p. 103-118. In M. Müller, R. P. Becker, A. Boyde, and J. J. Wolosewick (ed.), Science of biological specimen preparation. SEM Inc., AMF O'Hare, Chicago, Ill.
30. van Gemeren, I. A., W. Musters, C. A. M. J. J. van den Hondel, and C. T. Verrips. 1995. Construction and heterologous expression of a synthetic copy of the cutinase cDNA from Fusarium solani pisi. J. Biotechnol. 40:155-162.
31. Verbakel, J. M. A. 1991. Heterologous gene expression in the yeast Saccharomyces cerevisiae. Ph.D. thesis. Utrecht University, Utrecht, The Netherlands.
32. Verger, R., and G. H. de Haas. 1979. Interfacial enzyme kinetics of lipolysis. Annu. Rev. Biophys. Bioeng. 5:77-117.