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Volumn 420, Issue 1, 2012, Pages 119-123

Temperature dependent N-glycosylation of plasma membrane heat shock protein Hsp30p in Saccharomyces cerevisiae

Author keywords

Heat shock protein; Hsp30p; N glycosylation; Saccharomyces cerevisiae; Stress response

Indexed keywords

ACETIC ACID; FUNGAL ENZYME; GLUCOSE; HEAT SHOCK PROTEIN 30;

EID: 84859107593     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.02.126     Document Type: Article
Times cited : (7)

References (40)
  • 2
    • 79955530385 scopus 로고    scopus 로고
    • +-ATPase (Pma1) by dextrose and Hsp30 during exposure to thermal stress
    • +-ATPase (Pma1) by dextrose and Hsp30 during exposure to thermal stress. Indian J. Microbiol. 2011, 51:153-158.
    • (2011) Indian J. Microbiol. , vol.51 , pp. 153-158
    • Meena, R.C.1    Thakur, S.2    Chakrabarti, A.3
  • 3
    • 0026634082 scopus 로고
    • The plasma membrane of yeast acquires a novel heat-shock protein (hsp30) and displays a decline in proton-pumping ATPase levels in response to both heat shock and the entry to stationary phase
    • Panaretou B., Piper P.W. The plasma membrane of yeast acquires a novel heat-shock protein (hsp30) and displays a decline in proton-pumping ATPase levels in response to both heat shock and the entry to stationary phase. Eur. J. Biochem. 1992, 206:635-640.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 635-640
    • Panaretou, B.1    Piper, P.W.2
  • 4
    • 0028151517 scopus 로고
    • Induction of major heat-shock proteins of Saccharomyces cerevisiae, including plasma membrane Hsp30, by ethanol levels above a critical threshold
    • Piper P.W., Talreja K., Panaretou B., Moradas-Ferreira P., Byrne K., Praekelt U.M., Meacock P., Recnacq M., Boucherie H. Induction of major heat-shock proteins of Saccharomyces cerevisiae, including plasma membrane Hsp30, by ethanol levels above a critical threshold. Microbiology 1994, 140:3031-3038.
    • (1994) Microbiology , vol.140 , pp. 3031-3038
    • Piper, P.W.1    Talreja, K.2    Panaretou, B.3    Moradas-Ferreira, P.4    Byrne, K.5    Praekelt, U.M.6    Meacock, P.7    Recnacq, M.8    Boucherie, H.9
  • 5
    • 0032896994 scopus 로고    scopus 로고
    • Stress induction of HSP30, the plasma membrane heat shock protein gene of Saccharomyces cerevisiae, appears not to use known stress-regulated transcription factors
    • Seymour I.J., Piper P.W. Stress induction of HSP30, the plasma membrane heat shock protein gene of Saccharomyces cerevisiae, appears not to use known stress-regulated transcription factors. Microbiology 1999, 145:231-239.
    • (1999) Microbiology , vol.145 , pp. 231-239
    • Seymour, I.J.1    Piper, P.W.2
  • 6
    • 0032960606 scopus 로고    scopus 로고
    • The oligosaccharyl transferase complex from yeast
    • Knauer R., Lehle L. The oligosaccharyl transferase complex from yeast. Biochim. Biophys. Acta 1999, 1426:259-273.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 259-273
    • Knauer, R.1    Lehle, L.2
  • 7
    • 33751508817 scopus 로고    scopus 로고
    • N-glycan processing in ER quality control
    • Ruddock L.W., Molinari M. N-glycan processing in ER quality control. J. Cell Sci. 2006, 119:4373-4380.
    • (2006) J. Cell Sci. , vol.119 , pp. 4373-4380
    • Ruddock, L.W.1    Molinari, M.2
  • 9
    • 27944459619 scopus 로고    scopus 로고
    • Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit
    • Schwarz M., Knauer R., Lehle L. Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit. FEBS Lett. 2005, 579:6564-6568.
    • (2005) FEBS Lett. , vol.579 , pp. 6564-6568
    • Schwarz, M.1    Knauer, R.2    Lehle, L.3
  • 10
    • 61649089751 scopus 로고    scopus 로고
    • Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency
    • Schulz B., Aebi M. Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency. Mol. Cell. Proteomics 2009, 8:357-364.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 357-364
    • Schulz, B.1    Aebi, M.2
  • 11
    • 33750468309 scopus 로고    scopus 로고
    • Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases
    • Lehle L., Strahl S., Tanner W. Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases. Angew. Chem. Int. Ed. 1997, 45:6802-6818.
    • (1997) Angew. Chem. Int. Ed. , vol.45 , pp. 6802-6818
    • Lehle, L.1    Strahl, S.2    Tanner, W.3
  • 12
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius A., Aebi M. Intracellular functions of N-linked glycans. Science 2001, 291:2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 13
    • 3943059566 scopus 로고    scopus 로고
    • Role of N-linked glycans in the endoplasmic reticulum
    • Helenius A., Aebi M. Role of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 2004, 73:1019-1049.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 14
    • 64049096002 scopus 로고    scopus 로고
    • N-glycans are direct determinants of CFTR folding and stability in secretory and endocytic membrane traffic
    • Golzman R., Okiyoneda T., Mulvihill C.M., Rini J.M., Barriere H., Lukas G.L. N-glycans are direct determinants of CFTR folding and stability in secretory and endocytic membrane traffic. J. Biol. Chem. 2009, 184:847-862.
    • (2009) J. Biol. Chem. , vol.184 , pp. 847-862
    • Golzman, R.1    Okiyoneda, T.2    Mulvihill, C.M.3    Rini, J.M.4    Barriere, H.5    Lukas, G.L.6
  • 16
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • Scwarz F., Aebi M. Mechanisms and principles of N-linked protein glycosylation. Curr. Opin. Struct. Biol. 2011, 21:576-582.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 576-582
    • Scwarz, F.1    Aebi, M.2
  • 17
    • 0025765996 scopus 로고
    • Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding
    • Riederer M.A., Hinnen A. Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding. J. Bacteriol. 1991, 173:3539-3546.
    • (1991) J. Bacteriol. , vol.173 , pp. 3539-3546
    • Riederer, M.A.1    Hinnen, A.2
  • 18
    • 0028800891 scopus 로고
    • Cloning of the Candida glabrata TRP1 and HIS3 genes, and construction of their disruptant strains by sequential integrative transformation
    • Kitada K., Yamaguchi E., Arisawa M. Cloning of the Candida glabrata TRP1 and HIS3 genes, and construction of their disruptant strains by sequential integrative transformation. Gene 1995, 165:203-206.
    • (1995) Gene , vol.165 , pp. 203-206
    • Kitada, K.1    Yamaguchi, E.2    Arisawa, M.3
  • 19
    • 0031845220 scopus 로고    scopus 로고
    • The yeast dynactin complex is involved in portioning the mitotic spindle between mother and daughter cells during anaphase B
    • Kahana J.A., Schlenstedt G., Evanchuk D.M., Geiser J.R., Hoyt M.A., Silver P.A. The yeast dynactin complex is involved in portioning the mitotic spindle between mother and daughter cells during anaphase B. Mol. Biol. Cell 1999, 9:1741-1756.
    • (1999) Mol. Biol. Cell , vol.9 , pp. 1741-1756
    • Kahana, J.A.1    Schlenstedt, G.2    Evanchuk, D.M.3    Geiser, J.R.4    Hoyt, M.A.5    Silver, P.A.6
  • 20
    • 49649096905 scopus 로고    scopus 로고
    • Heat shock and ethanol stress provoke distinctly different responses in 3'-processing and nuclear export of HSP mRNA in Saccharomyces cerevisiae
    • Izawa S., Kita T., Ikeda K., Inoue Y. Heat shock and ethanol stress provoke distinctly different responses in 3'-processing and nuclear export of HSP mRNA in Saccharomyces cerevisiae. Biochem. J. 2008, 414:111-119.
    • (2008) Biochem. J. , vol.414 , pp. 111-119
    • Izawa, S.1    Kita, T.2    Ikeda, K.3    Inoue, Y.4
  • 21
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski R.S., Hieter P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Gene 1989, 122:19-27.
    • (1989) Gene , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 22
    • 79952572657 scopus 로고    scopus 로고
    • Modification of yeast characteristics by soy peptides: cultivation with soy peptides represses the formation of lipid bodies
    • Ikeda K., Kitagawa S., Tada T., Iefuji H., Inoue Y., Izawa S. Modification of yeast characteristics by soy peptides: cultivation with soy peptides represses the formation of lipid bodies. Appl. Microbiol. Biotechnol. 2011, 89:1971-1977.
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , pp. 1971-1977
    • Ikeda, K.1    Kitagawa, S.2    Tada, T.3    Iefuji, H.4    Inoue, Y.5    Izawa, S.6
  • 23
    • 0029127922 scopus 로고
    • Thermosensitivity of green fluorescent protein fluorescence utilized to reveal novel nuclear-like compartments in a mutant nucleoporin Nsp1
    • Lim C.R., Kimata Y., Oka M., Nomaguchi K., Kohno K. Thermosensitivity of green fluorescent protein fluorescence utilized to reveal novel nuclear-like compartments in a mutant nucleoporin Nsp1. J. Biochem. 1995, 118:13-17.
    • (1995) J. Biochem. , vol.118 , pp. 13-17
    • Lim, C.R.1    Kimata, Y.2    Oka, M.3    Nomaguchi, K.4    Kohno, K.5
  • 24
    • 0029586689 scopus 로고
    • Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells
    • Ogawa H., Inouye S., Tsuji F.I., Yasuda K., Umesono K. Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells. Proc. Natl. Acad. Sci. USA 1995, 92:11899-11903.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11899-11903
    • Ogawa, H.1    Inouye, S.2    Tsuji, F.I.3    Yasuda, K.4    Umesono, K.5
  • 25
    • 0017181626 scopus 로고
    • The specific site of tunicamycin inhibition in the formation of dolichol-bound N-acetylglucosamine derivatives
    • Lehle L., Tanner W. The specific site of tunicamycin inhibition in the formation of dolichol-bound N-acetylglucosamine derivatives. FEBS Lett. 1976, 72:167-170.
    • (1976) FEBS Lett. , vol.72 , pp. 167-170
    • Lehle, L.1    Tanner, W.2
  • 26
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics A., Orlean P. Glycoprotein biosynthesis in yeast. FASEB J. 1993, 7:540-550.
    • (1993) FASEB J. , vol.7 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 27
    • 0041856249 scopus 로고    scopus 로고
    • New findings on interactions among the yeast oligosaccharyl transferase subunits using a chemical cross-linker
    • Yan A., Ahmed E., Lennarz W.J. New findings on interactions among the yeast oligosaccharyl transferase subunits using a chemical cross-linker. J. Biol. Chem. 2003, 278:33078-33087.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33078-33087
    • Yan, A.1    Ahmed, E.2    Lennarz, W.J.3
  • 29
    • 0028846436 scopus 로고
    • + RNA in heat-shocked yeast cells: implication of nucleolar involvement in mRNA transport
    • + RNA in heat-shocked yeast cells: implication of nucleolar involvement in mRNA transport. Mol. Biol. Cell 1995, 6:1515-1534.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1515-1534
    • Tani, T.1    Derby, R.J.2    Hiraoka, Y.3    Spector, D.L.4
  • 30
    • 0029737693 scopus 로고    scopus 로고
    • Regulation of mRNA export in response to stress in Saccharomyces cerevisiae
    • Saavedra C., Tung K.S., Amberg D.C., Hopper A.K., Cole C.N. Regulation of mRNA export in response to stress in Saccharomyces cerevisiae. Genes Dev. 1996, 10:1608-1620.
    • (1996) Genes Dev. , vol.10 , pp. 1608-1620
    • Saavedra, C.1    Tung, K.S.2    Amberg, D.C.3    Hopper, A.K.4    Cole, C.N.5
  • 31
    • 4143089556 scopus 로고    scopus 로고
    • + mRNA to heat shock in Saccharomyces cerevisiae
    • + mRNA to heat shock in Saccharomyces cerevisiae. J. Biol. Chem. 2004, 279:35469-35478.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35469-35478
    • Izawa, S.1    Takemura, R.2    Inoue, Y.3
  • 32
    • 0026040203 scopus 로고
    • Inhibition of heat shock protein synthesis and protein glycosylation by stepdown heating
    • Henle K.J., Nagle W.A. Inhibition of heat shock protein synthesis and protein glycosylation by stepdown heating. Exp. Cell Res. 1991, 196:184-191.
    • (1991) Exp. Cell Res. , vol.196 , pp. 184-191
    • Henle, K.J.1    Nagle, W.A.2
  • 34
    • 0028128694 scopus 로고
    • Heat shock-induced prompt glycosylation. Identification of P-SG67 as calreticulin
    • Jethmalani S.M., Henle K.J., Kaushal G.P. Heat shock-induced prompt glycosylation. Identification of P-SG67 as calreticulin. J. Biol. Chem. 1994, 269:23603-23609.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23603-23609
    • Jethmalani, S.M.1    Henle, K.J.2    Kaushal, G.P.3
  • 37
    • 0023880441 scopus 로고
    • Effect of glycosylation on the mechanism of renaturation of invertase from yeast
    • Schülke N., Schmid F.X. Effect of glycosylation on the mechanism of renaturation of invertase from yeast. J. Biol. Chem. 1988, 263:8832-8837.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8832-8837
    • Schülke, N.1    Schmid, F.X.2
  • 38
    • 46749092844 scopus 로고    scopus 로고
    • N-glycosylation of the Drosophila neural protein Chaoptin is essential for its stability, cell surface transport and adhesive activity
    • Hirai-Fujita Y., Yamamoto-Hino M., Kanie O., Goto S. N-glycosylation of the Drosophila neural protein Chaoptin is essential for its stability, cell surface transport and adhesive activity. FEBS Lett. 2008, 582:2572-2576.
    • (2008) FEBS Lett. , vol.582 , pp. 2572-2576
    • Hirai-Fujita, Y.1    Yamamoto-Hino, M.2    Kanie, O.3    Goto, S.4
  • 39
    • 80052400203 scopus 로고    scopus 로고
    • N-glycosylation is critical for the stability and intracellular trafficking of glucose transporter GLUT4
    • Haga Y., Ishii K., Suzuki T. N-glycosylation is critical for the stability and intracellular trafficking of glucose transporter GLUT4. J. Biol. Chem. 2011, 286:31320-31327.
    • (2011) J. Biol. Chem. , vol.286 , pp. 31320-31327
    • Haga, Y.1    Ishii, K.2    Suzuki, T.3
  • 40
    • 67649625166 scopus 로고    scopus 로고
    • A genome-wide screen for genes affecting eisosomes reveals Nce102 function in sphingolipid signaling
    • Fröhlich F., Moreira K., Aguilar P.S., Hubner N.C., Mann M., Walter P., Walther T.C. A genome-wide screen for genes affecting eisosomes reveals Nce102 function in sphingolipid signaling. J. Cell Biol. 2009, 185:1227-1242.
    • (2009) J. Cell Biol. , vol.185 , pp. 1227-1242
    • Fröhlich, F.1    Moreira, K.2    Aguilar, P.S.3    Hubner, N.C.4    Mann, M.5    Walter, P.6    Walther, T.C.7


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