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2008 | 13 | 4 |

Tytuł artykułu

The effect of calnexin deletion on the expression level of binding protein [BiP] under heat stress conditions in Saccharomyces cerevisiae

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
We cultured calnexin-disrupted and wild-type Saccharomyces cerevisiae strains under conditions of heat stress. The growth rate of the calnexin-disrupted yeast was almost the same as that of the wild-type yeast under those conditions. However, the induced mRNA level of the molecular chaperone PDI in the ER was clearly higher in calnexin-disrupted S. cerevisiae relative to the wild type at 37°C, despite being almost the same in the two strains under normal conditions. The western blotting analysis for PDI protein expression in the ER yielded results that show a parallel in their mRNA levels in the two strains. We suggest that PDI may interact with calnexin under heat stress conditions, and that the induction of PDI in the ER can recover part of the function of calnexin in calnexin-disrupted yeast, and result in the same growth rate as in wild-type yeast.

Wydawca

-

Rocznik

Tom

13

Numer

4

Opis fizyczny

p.621-631,fig.,ref.

Twórcy

autor
  • Liaoning University, Shenyang 110036, China
autor
autor
autor
autor

Bibliografia

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  • 3. Letourneur, O., Sechi, S., Willete-Brown, J., Robertson, M.W. and Kinet J.P. Glycosylation of human truncated Fc epsilon RI alpha chain is necessary for efficient folding in the endoplasmic reticulum. J. Biol. Chem. 270 (1995) 8249-8256.
  • 4. Degen, E., Cohen-Doyle, M.F. and Williams, D.B. Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide. J. Exp. Med. 175 (1992) 1653-1661.
  • 5. Hammond, C., Braakman, I. and Helenius, A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA 91 (1994) 913-917.
  • 6. Jackson, M.R., Cohen-Doyle, M.F., Peterson, P, A. and Williams, D.B. Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Science 263 (1994) 384-387.
  • 7. Ware, F.E., Vassilakos, A., Peterson, P.A., Jackson, M.R., Lehrman, M.A. and Williams, D.B. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem. 270 (1995) 4697-4704.
  • 8. Parlati, F., Dominguez, M., Bergeron, J.M. and Thomas, D.Y. Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J. Biol. Chem. 270 (1995) 244-253.
  • 9. Jakob, C.A., Burda, P. S., te Heesen, S., Aebi, M. and Roth, J. Genetic tailoring of N-linked oligosaccharides: the role of glucose residues in glycoprotein processing of Saccharomyces cerevisiae in vivo. Glycobiology 8 (1998) 155-164.
  • 10. Mori, K., Ogawa, N., Kawahara, T., Yanagi, H. and Yura, T. Palindrome with spacer of one nucleotide is characteristic of the cis-acting unfolded protein response element in Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998) 9912-9920.
  • 11. Song. Y., Sata, J., Saito, A., Usui, M., Azakami, H. and Akio, K. Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes. J. Biochem. 130 (2001) 757-764.
  • 12. Gething, M.J. and Sambrook, J. Protein folding in the cell. Nature 355 (1992) 33-45.
  • 13. Helenius, A., Tatu, U., Marquardt, T. and Braakman, I. Protein folding in the endoplasmic reticulum. In: Cell Biology and Biotechnology (Rupp, R.G. and Oka, M.S.), Berlin/Heidelberg, Springer Verlag, 1992.
  • 14. Lee, A.S. Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells. Trends Biochem. Sci. 12 (1987) 20-23.
  • 15. Kozutsumi, Y., Segal, M., Normington, K., Gething, M.J. and Sambrook, J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332 (1988) 462-464.
  • 16. Molinari, M. and Helenius, A. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 288 (2000) 331-333.
  • 17. Pirneskoski, A., Ruddock, L.W., Klappa, P., Freedman, R.B., Kivirikko, K.I. and Koivunen, P. Domains b’ and a’ of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. J. Biol. Chem. 276 (2001) 11287-11293.
  • 18. Williams, D.B. Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J. Cell. Sci. 119 (2006) 615-623.
  • 19. Parlatill, F., Dignard, D., Bergeron, J.J.M. and Thomas, D.Y. The calnexin homologue cnx1+ in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain. EMBO J. 14 (1995) 3064-3072.
  • 20. Siebert, P.D. and Larrick, J.W. Competitive PCR. Nature 359 (1992) 557-558.
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  • 22. Lamantia, M., Miura, T., Tachikawa, H., Kaplan, H.A., Lennarz, W.J. and Mizunaga, T. Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast. Proc. Natl. Acad. Sci. USA 88 (1991) 4453-4457.
  • 23. Arima, H., Kinoshita, T., Ibrahim H.R., Azakami, H. and Kato, A. Enhanced secretion of hydrophobic peptide fused lysozyme by the introduction of N-glycosylation signal and the disruption of calnexin gene in Saccharomyces cerevisiae. FEBS Lett. 440 (1998) 89-92.
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Typ dokumentu

Bibliografia

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Identyfikator YADDA

bwmeta1.element.agro-article-f90ace39-9810-4398-903d-4b5a4a90fec4
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